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Database: UniProt
Entry: D2V1F0_NAEGR
LinkDB: D2V1F0_NAEGR
Original site: D2V1F0_NAEGR 
ID   D2V1F0_NAEGR            Unreviewed;      1284 AA.
AC   D2V1F0;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=Predicted protein {ECO:0000313|EMBL:EFC49155.1};
GN   ORFNames=NAEGRDRAFT_45871 {ECO:0000313|EMBL:EFC49155.1};
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:EFC49155.1, ECO:0000313|Proteomes:UP000006671}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NEG-M {ECO:0000313|EMBL:EFC49155.1,
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; GG738848; EFC49155.1; -; Genomic_DNA.
DR   RefSeq; XP_002681899.1; XM_002681853.1.
DR   STRING; 5762.D2V1F0; -.
DR   EnsemblProtists; EFC49155; EFC49155; NAEGRDRAFT_45871.
DR   GeneID; 8855157; -.
DR   VEuPathDB; AmoebaDB:NAEGRDRAFT_45871; -.
DR   eggNOG; KOG2715; Eukaryota.
DR   InParanoid; D2V1F0; -.
DR   OrthoDB; 2912088at2759; -.
DR   Proteomes; UP000006671; Unassembled WGS sequence.
DR   GO; GO:0009882; F:blue light photoreceptor activity; IEA:InterPro.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
DR   Gene3D; 3.30.530.20; -; 1.
DR   Gene3D; 3.30.70.100; -; 1.
DR   Gene3D; 1.10.167.10; Regulator of G-protein Signalling 4, domain 2; 1.
DR   InterPro; IPR036046; Acylphosphatase-like_dom_sf.
DR   InterPro; IPR045068; BACURD1-3.
DR   InterPro; IPR007024; BLUF_domain.
DR   InterPro; IPR016137; RGS.
DR   InterPro; IPR036305; RGS_sf.
DR   InterPro; IPR044926; RGS_subdomain_2.
DR   InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR   InterPro; IPR023393; START-like_dom_sf.
DR   InterPro; IPR003131; T1-type_BTB.
DR   PANTHER; PTHR11145:SF8; BTB DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR11145; BTB/POZ DOMAIN-CONTAINING ADAPTER FOR CUL3-MEDIATED RHOA DEGRADATION PROTEIN FAMILY MEMBER; 1.
DR   Pfam; PF04940; BLUF; 1.
DR   Pfam; PF02214; BTB_2; 2.
DR   SMART; SM01034; BLUF; 1.
DR   SUPFAM; SSF54975; Acylphosphatase/BLUF domain-like; 1.
DR   SUPFAM; SSF55961; Bet v1-like; 1.
DR   SUPFAM; SSF54695; POZ domain; 2.
DR   SUPFAM; SSF48097; Regulator of G-protein signaling, RGS; 1.
DR   PROSITE; PS50925; BLUF; 1.
DR   PROSITE; PS50132; RGS; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006671}.
FT   DOMAIN          651..747
FT                   /note="RGS"
FT                   /evidence="ECO:0000259|PROSITE:PS50132"
FT   DOMAIN          1131..1226
FT                   /note="BLUF"
FT                   /evidence="ECO:0000259|PROSITE:PS50925"
FT   REGION          940..961
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          37..97
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          261..311
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1284 AA;  149901 MW;  A303AF43A00E33DE CRC64;
     MPRTNPGAQK KRSNSAIDLT EEDEVVQISD EEEEVIKKRN ERLLQKQREA MIRYERAQSE
     TSFNEEFTQI ASELYTLTKH NESMETLITQ IDRLNIKDPM EETEKSKIDL LAEQIIKQSD
     DIVSFNVSGQ VFTTTKGTIR REKESFLTVL IDENSHLPFD TDESGAFIIE RSALLFSYIL
     KYLQNLDEFT GEFDIDILPK EKTVLNALLE EAKFFSLSNL IEVLDKNNSA QMLEGRSAAR
     LVDVWNYGNI VRDAVVSDEY LDQIKERVQR RKEQLNQQRE MIKNLVENQQ KKQVETRRNE
     LESKLAQIRQ DLGKVDSLTV FFSISGTIFE MDIFQVFKFK ESLLCKIVQK YNIPIQETKS
     RPIFIDREPE QFTHIKYFIE NECLSEDLLY GRSYNKKALL KEAAFYNITD LVKYLDPVYR
     FPIEELGSHN VVMKREEDLL RSYFATNRDH PLLSDPYLHL INVFDNLDTF KKQPFPDRGN
     ILFKQYSDHL FVESREEFEF NFNCFTKGIF NVKADFTNSR GLARLLLLEK KSTYILGEKD
     QRVTENTIIK FTAEERQKLL FNNWDMDSDY LGVLIAFKYR GVPTFFSDLL EMLQSGLTQT
     KLIMTVDEIE TILNIPDQKL AQCELTKRIE WIKIDPDSSC NIMNESATNY EDYQFSFEKL
     YREKETRLLM KEYMEMEMEV NIGRKEKEVV MLKYKQLQSQ WSESSSAILE PVKIWEIFEE
     ARIVIMTELK QDVFPRFIRS QRFISFIQTH DKEFLDKIGL NLGRRISDTV SVSSDESSGN
     STTQRKKVTV DYSVRPEFYW KNYQADASIH NITQQDVKFV NSLTLDSNIW QLFKVGDKKK
     GEYFASFVSK QKLSVFKPDS TTERQVNPQK LYKFTGVINH SLEELLFTLT NPAYMMDYDN
     QLSVVEQLDY LNGFDYSSSI SVQGSSSAFW ENENFDDSSS DGGLSVDSQS STSPKVSHSD
     DKFSSSICLE TYPFGWPISN RDFLVTQSLI YEAKTQRYIL VKKSISHPNY PKRKGTTRGF
     IVGGWTIQRV TENQTRFCFV SFTDMDLNER VFNQLCKKKG KRLFDGLNQT LDRNSENGFL
     RPLFSCGLLE TLEDFLKFYK LPETILNETQ VQVLKKQKSD KFKSFEIDGS LVRLIYVSRY
     DESKLSSKDF DQINQVSNRN NQPLNLSGIL LSGQGVFYQV LEGDPKFIYP TYERIKKDSR
     HFDVWCVSEE SGVKECERQF SNWAMKCVDL VNSDHYLAQF MRNIIETLSK LSKASRDSTN
     WDEENHALDV LYQASKQLND SSKN
//
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