ID D2VJS7_NAEGR Unreviewed; 732 AA.
AC D2VJS7;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EFC43002.1};
GN ORFNames=NAEGRDRAFT_69147 {ECO:0000313|EMBL:EFC43002.1};
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:EFC43002.1, ECO:0000313|Proteomes:UP000006671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEG-M {ECO:0000313|EMBL:EFC43002.1,
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; GG738876; EFC43002.1; -; Genomic_DNA.
DR RefSeq; XP_002675746.1; XM_002675700.1.
DR AlphaFoldDB; D2VJS7; -.
DR STRING; 5762.D2VJS7; -.
DR EnsemblProtists; EFC43002; EFC43002; NAEGRDRAFT_69147.
DR GeneID; 8853140; -.
DR VEuPathDB; AmoebaDB:NAEGRDRAFT_69147; -.
DR eggNOG; KOG0039; Eukaryota.
DR InParanoid; D2VJS7; -.
DR OrthoDB; 2787294at2759; -.
DR Proteomes; UP000006671; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd09631; DOMON_DOH; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR InterPro; IPR045266; DOH_DOMON.
DR InterPro; IPR005018; DOMON_domain.
DR InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR InterPro; IPR013121; Fe_red_NAD-bd_6.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR PANTHER; PTHR11972:SF69; METALLOREDUCTASE AIM14-RELATED; 1.
DR PANTHER; PTHR11972; NADPH OXIDASE; 1.
DR Pfam; PF03351; DOMON; 1.
DR Pfam; PF01794; Ferric_reduct; 1.
DR Pfam; PF08030; NAD_binding_6; 1.
DR SMART; SM00664; DoH; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR PROSITE; PS50836; DOMON; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000006671};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 41..60
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 260..282
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 325..344
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 364..385
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 397..417
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 423..448
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 460..480
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 486..507
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 572..591
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 83..210
FT /note="DOMON"
FT /evidence="ECO:0000259|PROSITE:PS50836"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 732 AA; 82322 MW; 007E932A8C5DE22E CRC64;
MKRETFKVHA IQQGRRNNDS TPSSSYSEGF LKMKKNVNNS LMMLVALISI MLLLGFSQYV
EALNGEGVDV SKCTYQSSVS LGSTMTLKWN VLKNPSDASN YILEFGLICT KAGYCSIGFD
HPYGQGMQSI DTLFAFVSSG VANVQDCYCT NKHSIPTIDS NNGGSNDFLE TNGGVVNGQY
HYRWSRKMST GDSQDATFKN SNVYVSWAYH SSSTSISSTH TDYGRNIAVN FLSNTPTETY
VKGMINNGAS ILVAPLTHKF HLYALAIGIA SLIMAGLIVT YLPTAFKSNI ITHFLFYRKI
SKVIPYDFPL VSYVNQFLDL TIGEVLVIIV YLAMKVVWFV YGFLTQTDDS TAKKVASGFT
QLIVFNYIFL FIPVTRYSVL QALFGISFER SIKFHKWIGV MVFLSATAHG IVEFIAYRDN
IPYIFSVGDG FPLLGIIAWL TLGLLLLFSL EPIRRKLYEL FLVFHIPLTF ITVTFSIIHG
EGWINLLPYM AFSLFLMVVD FLLRAIIGFG VPTKLVQISY DEDAEVTTCV FEKRFLTLFH
NPNHAHFVFV YIPQVSIYQL HPMTIKDPKR TIVFIVAGIG ATPANAILTA LEDPKYNEPT
PYKVFVNFTM RNEALLPHLT KIIQQKPNVE SSFYITGSKS KSHNANQIEM LEKGRSTGID
HSNDRRFIKG SRPVYEEYLH KVKQYVAQSK SKPYVSVFAC GPAAMMNAVH NAVISASDMD
CRFELHKEEF EF
//
