ID D2VSK5_NAEGR Unreviewed; 1000 AA.
AC D2VSK5;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=EGF-like domain-containing protein {ECO:0000259|PROSITE:PS50026};
GN ORFNames=NAEGRDRAFT_59108 {ECO:0000313|EMBL:EFC40207.1};
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:EFC40207.1, ECO:0000313|Proteomes:UP000006671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEG-M {ECO:0000313|EMBL:EFC40207.1,
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; GG738894; EFC40207.1; -; Genomic_DNA.
DR RefSeq; XP_002672951.1; XM_002672905.1.
DR AlphaFoldDB; D2VSK5; -.
DR STRING; 5762.D2VSK5; -.
DR EnsemblProtists; EFC40207; EFC40207; NAEGRDRAFT_59108.
DR GeneID; 8854682; -.
DR VEuPathDB; AmoebaDB:NAEGRDRAFT_59108; -.
DR eggNOG; KOG1225; Eukaryota.
DR InParanoid; D2VSK5; -.
DR OMA; CANVECA; -.
DR OrthoDB; 5471657at2759; -.
DR Proteomes; UP000006671; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR Gene3D; 2.10.25.10; Laminin; 9.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
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; 12.
DR SUPFAM; SSF101898; NHL repeat; 1.
DR PROSITE; PS00022; EGF_1; 6.
DR PROSITE; PS01186; EGF_2; 3.
DR PROSITE; PS50026; EGF_3; 4.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000006671};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..1000
FT /note="EGF-like domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003038365"
FT TRANSMEM 947..977
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 300..339
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 420..459
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 500..539
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 688..727
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 329..338
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 449..458
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 529..538
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 717..726
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1000 AA; 107374 MW; F67EDC321DA79377 CRC64;
MLNNNKWVVI NSIVLIFSLL FVFPHLTKSA DVKFKIRTVV DSLVKPTSVS VFENGDIYVA
EESVVSKIYT NGTKVIVAGG GSDTSSAVMV PTQAQLNIYF SSFDCIGKPG AYGSASSGTY
FLKNLSSPKG IFRTSKNEFY IAESSGRVKV YNGTLRQIAG VGLIGSSCPD DSDALTCLIS
NTNGIFVSGK NEVYITEMIA SGTVRKLYPY CEDGLVLSSD GRLCNPLCFT KSGNEACGGP
SHGLCIDVDT CQCNNNYYGM ACELPKCFGK NSTLYCSMNG ECIDVNNCSC NSNYYGIECN
VTTCDGKFSN NSNTCSNHGT CVDYNICECN ENYEGTFCNI SKCNGTLSND PSVCSGNGNC
LEYDTCQCFN SSMYSGSFCE IPICFGILAN QSLSVCSGQG NCISVDQCQC NSKYGGSQCE
IPFCNTKLGT DPLVCNSHGN CTAPNQCQCM SGYDGSECEL INCFGIYSNQ TNQICNQGNG
TCLAPDTCSC NSGWTGLNCE IPICHGVPSN NSRACSSNGQ CTNPNYCKCD SNYYGTNCEK
TTCNSVPSDD SNVCFGNGKC ISYNNCNCSD GYGPSTTCQF PICFGKLAND SSVCNDTEQY
CDAPNECKLK NPICFGIEKL DNRSCSGNGK CLSTDYCKCD FNYFGEECQY FKCNGVEFNS
TRVCNSHGVC KFLNTCICEN GFGGNNCELV ECNGILESSS SVCSGRGTCL NVDQCECEYG
YSGSNCQFTS CFGIEQESSQ VCNLGNGTCR SFDYCKCVNE SKWFGPQCNI TYCYGETSVD
SKVCSSQGDC VNYDTCHCKK DFIGNKCQFK FLSQAMKLSF NNTSDIVGDI STIISLSIQD
SSFLDYYVNQ SINIFIEFLL DGQFDSSSTV HQQLTSSIPF NLPASLSKTG SLTAKAALSL
NSTLISFRVE TETALSLQLK NIPQISARLT SLPFLAIDSV HSENTGVIVA AVVVPIVSVA
VIGGGVAVLI TTIVIMMKKK ASASLAKDLI MAGATDVELA
//