GenomeNet

Database: UniProt
Entry: D2V0Y2_NAEGR
LinkDB: D2V0Y2_NAEGR
Original site: D2V0Y2_NAEGR 
ID   D2V0Y2_NAEGR            Unreviewed;      1833 AA.
AC   D2V0Y2;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=Predicted protein {ECO:0000313|EMBL:EFC49596.1};
GN   ORFNames=NAEGRDRAFT_62456 {ECO:0000313|EMBL:EFC49596.1};
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:EFC49596.1, ECO:0000313|Proteomes:UP000006671}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NEG-M {ECO:0000313|EMBL:EFC49596.1,
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   -!- SIMILARITY: Belongs to the TOG/XMAP215 family.
CC       {ECO:0000256|ARBA:ARBA00025722}.
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DR   EMBL; GG738847; EFC49596.1; -; Genomic_DNA.
DR   RefSeq; XP_002682340.1; XM_002682294.1.
DR   STRING; 5762.D2V0Y2; -.
DR   EnsemblProtists; EFC49596; EFC49596; NAEGRDRAFT_62456.
DR   GeneID; 8855480; -.
DR   VEuPathDB; AmoebaDB:NAEGRDRAFT_62456; -.
DR   eggNOG; KOG1820; Eukaryota.
DR   InParanoid; D2V0Y2; -.
DR   OMA; VCEYVRE; -.
DR   OrthoDB; 5479337at2759; -.
DR   Proteomes; UP000006671; Unassembled WGS sequence.
DR   GO; GO:0043232; C:intracellular non-membrane-bounded organelle; IEA:UniProt.
DR   GO; GO:0099080; C:supramolecular complex; IEA:UniProt.
DR   GO; GO:0061863; F:microtubule plus end polymerase; IEA:InterPro.
DR   GO; GO:0051010; F:microtubule plus-end binding; IEA:InterPro.
DR   GO; GO:0030951; P:establishment or maintenance of microtubule cytoskeleton polarity; IEA:InterPro.
DR   GO; GO:0046785; P:microtubule polymerization; IEA:InterPro.
DR   GO; GO:0007051; P:spindle organization; IEA:InterPro.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 4.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR019399; Parkin_co-regulated_protein.
DR   InterPro; IPR034085; TOG.
DR   InterPro; IPR045110; XMAP215.
DR   InterPro; IPR048491; XMAP215_CLASP_TOG.
DR   PANTHER; PTHR12609:SF0; CYTOSKELETON-ASSOCIATED PROTEIN 5; 1.
DR   PANTHER; PTHR12609; MICROTUBULE ASSOCIATED PROTEIN XMAP215; 1.
DR   Pfam; PF21040; CEP104-like_TOG; 1.
DR   Pfam; PF10274; ParcG; 1.
DR   Pfam; PF21041; XMAP215_CLASP_TOG; 1.
DR   SMART; SM01349; TOG; 4.
DR   SUPFAM; SSF48371; ARM repeat; 2.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000006671}.
FT   DOMAIN          170..391
FT                   /note="TOG"
FT                   /evidence="ECO:0000259|SMART:SM01349"
FT   DOMAIN          418..654
FT                   /note="TOG"
FT                   /evidence="ECO:0000259|SMART:SM01349"
FT   DOMAIN          725..961
FT                   /note="TOG"
FT                   /evidence="ECO:0000259|SMART:SM01349"
FT   DOMAIN          977..1214
FT                   /note="TOG"
FT                   /evidence="ECO:0000259|SMART:SM01349"
FT   REGION          1..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          67..161
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          651..707
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1213..1298
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1641..1664
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..50
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        67..98
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        126..161
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        666..707
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1213..1237
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1238..1268
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1274..1298
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1833 AA;  205740 MW;  5E221C3466DC959D CRC64;
     MLEEELRKEE ERMKNKSQKP KISSNNSDKL LRPPSASTSL NPPPANISPT ASVELSNFLI
     SSKNINNFIS DAPPVNIPTE ENNNSEISSP TSETIKTSSS TVKEEKNSKP STPASDIKVG
     TVPKKQNPIN KPSPQNELNK SIPIPENNLN GDSASSSQDS TTLFETLLKE ELERSKQQSE
     GGEDKPAWAK KVDELDELIT KFKTKDTNDS IFQDSETELT QTLNNRHPNI LEKGVETLFH
     YVNRYQNVQN SAEKFINLLV DKGLSSKSSV QQKSTDIILL YFETCDPAAI LTVLKAFFSS
     KKAKVRSQCI GIVKSAVQCF GFPTIPPKMI LQSLPTILED ASSREESHKL AIETFKWLGY
     ETVEPHLKDV KGSKLKALKD EYDLLQDKSP KPTRFSRLAS VYNSTASIKN LVTAASEELK
     AKREIIDLND KIRKDWYDDV TNAKWIIKRD ALKELKQLLE TFNIKKADYS EILSQINVII
     QREKNVVVVK ESIECLSAFS KALKTDFTSS AKPFYERLLT KLKEKNLSDS TIECLVSFDV
     SSFPFTDMLE TIFSAMNNKT ASTSEKLQIF TFIDKCFQNK KKKDLEKALK NLVNNLLSFC
     EDASSEVRDL CCKTLARLLF IIGDTDYTNL FLKLDSYMKE KIVQYLESYG SPPSDGVGKK
     LSQSIEKKTA PANIPKTTSS VTLRPSSRAD TNPVRSSTSS LAKKPSSKPL VSKSISLKKT
     ESIQSLSSSD VIEEANNLFG GNIVEQLANS NWNDRMLSLN HIESVISSLD KNDLQTKHEH
     IISLFQYKPG TKESNAKVLE KIFEIIERVL SSTEGKLSEV NIPPTLQWMI EKLATPKVDI
     IIQKAMKKVC ESINPQFVFN KISETLTDKM PPKLIGSVLE WLGEVITEFS IACFNSSELI
     EFSKKYLGNS NPIIKKGCIK MLCSMKLFMG EGLLNFLGDV KPALLDMVKK DFSKVDSKPP
     EPTRKVKGEQ LKVSSAMYDT LPRCDILPKL HPKIYHSMED KNWMTRLEAI QTVEKIIVND
     AHKRILPNIL ELIHALRQRL EDNNNKVVIS TLLLIDLISE AVGPEMEKFI KILLPSVISK
     SMHNNKAVRT CALESLEKYL NIVQFESMLK IFPKSIASDK GNPEGKKEII EFMHKHIVEM
     KNKNVDLFTP LVKPILDYLT KAGSDTRKLA EAILGEIISN GGYDFVFKRI RELKAAHQKG
     FSLLLQKYAP STEVESQPPP VTQSLTLPTT PSNSIRGDKK ITLRDVSKSL SVDTRQTEEE
     EGSKVPKTVK KRANISKTLA TSPNKSPSPS SPKTKPITNT FVPKLQFSTG ITGIATVDEY
     KLDLDKIEVN HDSPVEAETP MHDVYNSANG PMPGNITPRM PERSPVRDNK KEELISGHSI
     GELVKAINTN DHGSEIAINA LKTLVSMFKD ESCRPAILSY LKELVESLTD NTQYSFEKAS
     AGLVSTRICK YLLSTLMQLF SNRQMAAFVP QETLQRMIDQ LLSRLLDERL PSLDYGQELL
     RGLNSLMLKV LENSNRTYSY TSLIHLLEYS YANTSLKKYT ELVVKCLIKL TKALAATIDR
     VDVDILLMDL HSFLTHNPPT FFKDRNDLPL RTIKTILNEL VKVKGETIRS CLGLIPTHKN
     PLIISYIELM VNSAQTTVSS STNSQATVPS TTTPNITAQT ISKPPRNSVT ASQIQQAYPL
     QQPSTVSNEK IVQDELTDIF NLISNKDSTH TGLYRLYEFK KNHPSVGINN HLLKCSEPFQ
     QYIHRQLAKI AQYESSKQES FAASSHRAQS PASRQRQATA ITSVDDIRRQ LKLHQQESKQ
     KNMGRSLTVS DLKKRIQNIE EKLSSTDNET TEE
//
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