ID D2VKL1_NAEGR Unreviewed; 2342 AA.
AC D2VKL1;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EFC42614.1};
GN ORFNames=NAEGRDRAFT_80323 {ECO:0000313|EMBL:EFC42614.1};
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:EFC42614.1, ECO:0000313|Proteomes:UP000006671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEG-M {ECO:0000313|EMBL:EFC42614.1,
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).
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DR EMBL; GG738878; EFC42614.1; -; Genomic_DNA.
DR RefSeq; XP_002675358.1; XM_002675312.1.
DR EnsemblProtists; EFC42614; EFC42614; NAEGRDRAFT_80323.
DR GeneID; 8852048; -.
DR VEuPathDB; AmoebaDB:NAEGRDRAFT_80323; -.
DR eggNOG; KOG0619; Eukaryota.
DR eggNOG; KOG4424; Eukaryota.
DR InParanoid; D2VKL1; -.
DR OrthoDB; 2909504at2759; -.
DR Proteomes; UP000006671; Unassembled WGS sequence.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR PANTHER; PTHR12673; FACIOGENITAL DYSPLASIA PROTEIN; 1.
DR PANTHER; PTHR12673:SF159; RAC GUANINE NUCLEOTIDE EXCHANGE FACTOR JJ; 1.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00015; IQ; 9.
DR SMART; SM00369; LRR_TYP; 3.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50096; IQ; 4.
DR PROSITE; PS51450; LRR; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Reference proteome {ECO:0000313|Proteomes:UP000006671};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1885..2089
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT REGION 1416..1456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1716..1741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1761..1781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2244..2295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1861..1888
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1761..1775
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2251..2295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2342 AA; 266257 MW; CF8309341454E33B CRC64;
MAALGLIYFV CTLFIGVAAF VWRKFFSSNA NNTTTTTTTS SSSTSTLGDE LVQKDVSSKV
SPRVLETGRK EEEILDETLK SVLEESGIFI ETNDVKEEPI SVEESSDETL SEVKTDEIQE
ELEEVSTPQQ EEEYQETFTE EKQISIPEEL SETCQEEILS QTKDITDMKE EEHLTDITES
QQKDITEEEI VEDSTTAVED NAKESIVVPT IVTEVKEEKS EPSELYITCL IVLQAIIRGY
LQRHSMGQVK ETLSMITQGL LNSFNIRSEL EEEKNSLTTM QSIVRNSNSV RKFMDEKQKV
QLIQAFIQSK LEFVKSSEQK DKVIELQSIL KSKLLMKNLK SLLESVSTLQ SFLHSKIVEE
NYVSTVSTIQ SLQARVRSNY ESKQVEEGLK SLEILQSRCL KSIVEKDLRN QLEKITILQS
KARTFIIGKK LRNEIENCKL IQSACTAYLK QKQILHLENL SSMIHSFAAS KQDRLNYRNN
VDNVKTLESV MRGYSQRNSM TNVLHAITDL QSHLIGQNSR KSLHKSIDRA NTLLALSKAK
CYKKSLMVDK SRLVILQALA RSSITNRKLN AKQASEEDLA LLVQSLHNGS KLRSEHSEKV
RSVNLINSLL SATKSRNTFN KEKLSIQTIQ AALNSHKVQH LHSNDMSNIG LIQSVIIAKK
ANDVKTTATN NIILLQSLIR GRQIQKEKSH NLDHAHVLTA FSKGRLMLHL FESQVATTTK
IQSFTRQYTS RKQMMKEIDN VCLLESLCTG FVERRNLSTE ISNILQCQSL IRGFMTRKVR
VSDDQIDQLE KKTHFVSMIQ SSMDGRNIRK IREQAAAHVK LFQAVSRAFL TLDSYQQQQI
ISLHLQSICR SVMERKALST DLNNLLGLQA LCRSRLITNR SKVDKNRVQI VQSNIRRYLA
HKHLDQEKLR VANLQSLIRG FANKQFVKDQ IARVTVMQSM TRAYSYRKQM KNSQSRINIL
QAKIRGYLEK TRIEGQNSLS NNLGSVMKGF AQRVKLFKAI TSTIPTIQSS VRQFALRKGI
SESLGAIINI QSLCRKHLQS ESKPLSLNRI LSLQALIRTY SKGKHTNQQL GKIPYIQALF
RGKQARKTIV KSSDVSPIQA VARSLKQRRV MEQSEQGITK ISAALLGYSK RRELFQSMKN
ITHCQTILKT VLSSNDLRSQ TKQSLDLISN LQQKLKTRLE LERFEKKKKS SLLLQSLARG
CTIRKFIRNS VKPSVELIDS LCIGHIEREN HRDKVEKATL LQSISRRAQA CNQISEQRQK
LLLLQAAFKS WKTRDTFKKE LEDKIIHELE DKIKRVVVIQ GFVRGYLFRR DNLLYTKRRQ
ESPTQQISEL PSTAEILRQL YQNDEFGDNE DSEEEVQLEY PEEADDIPEP VIIEEPHVEV
TVNSFLDTPS SPEELPSIIP IPLHRRTSNA PLPAINITAS TPTPTTTVTP SVFSKEPVGI
TSSTKNTRLP SQKPPTRRQL IQNIIEECKR TKNPVLNLSG YDLETLPYSA IDCKHVTELI
LSQNNLVTLP SWFVDTFSDL KVLDLSGNQL YELPIDLARL SLTSINLSNN KLEFLPQALN
EMNTLTKIDI SENVLLSLPS TISHLVNVEE LDISNNYLMT LPDDIKKLKK LKNFQYYNNE
YLQSEISKIA EVISAVSGEK AKTIIQKLRN EDSMGYKEIG LSNKHKENNL FLDPYDLTDM
SEATEMYNGE DGESDYSMTD DVVLSPRLMR NNSSATMVET DTTSTPMTPI SGRNNDYLDT
PPTHTLSVTT EEYGTPCITP PAISDSDSES DVTPPKYNPP VTIPQIKLEV IENLDSPSSS
PAEHSPISMH PPKVIMTEED KKVNFGQLNK EGNEKSLTDV VHMEHPLFAT PKIRPVSASY
KKVALEESEE ERKEREAKEN KKSKERINMV LEILESERKY VKYLDVLWDL FYEPIVNNYF
PADKNKNPEE SERLVPKMIA KNFFPNDLLT IKTFNKNFLV KLEDRFKIYK GDPTKIYDML
IGDLFEKIAP FFKIYTSYLS SYESTMNKIR EYRAEDKIFD KWLDKRKTHP RCAGLEIGSF
LIMPVQRIPR YKLLLENLCK NTPPDHADYS NLISAIEKIT ESATTQNAKI KETNNRIKVY
QLSRLMKLSD LVQPHRRLIR EGEIVFGDQP KIEYKAYLFN DIFVFREKKR QKTKVAKSVK
AYSLLDAFIS GGGQNRLSMI LLNAEKNKTV EKEILFPSHE VKMEWVLEIE KALEEVREKR
ELISKGTKAI VRTSSRAGRF FRALKSPGRK GDLSPTSSNL SSTTIGQPST PSTSAPELRG
VTRTNSTVSD QSTTSVVSNL SVISSTSNVA SSSTSSLSSS SDGKKKSILG KIMMGFATNK
KK
//
