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Database: UniProt
Entry: D2UZK3_NAEGR
LinkDB: D2UZK3_NAEGR
Original site: D2UZK3_NAEGR 
ID   D2UZK3_NAEGR            Unreviewed;      1250 AA.
AC   D2UZK3;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   SubName: Full=Vacuolar protein sorting protein {ECO:0000313|EMBL:EFC50169.1};
GN   ORFNames=NAEGRDRAFT_56631 {ECO:0000313|EMBL:EFC50169.1};
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:EFC50169.1, ECO:0000313|Proteomes:UP000006671}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NEG-M {ECO:0000313|EMBL:EFC50169.1,
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:ARBA00004287};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004287};
CC       Cytoplasmic side {ECO:0000256|ARBA:ARBA00004287}.
CC   -!- SIMILARITY: Belongs to the VPS18 family.
CC       {ECO:0000256|ARBA:ARBA00010454}.
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DR   EMBL; GG738846; EFC50169.1; -; Genomic_DNA.
DR   RefSeq; XP_002682913.1; XM_002682867.1.
DR   AlphaFoldDB; D2UZK3; -.
DR   STRING; 5762.D2UZK3; -.
DR   EnsemblProtists; EFC50169; EFC50169; NAEGRDRAFT_56631.
DR   GeneID; 8855354; -.
DR   VEuPathDB; AmoebaDB:NAEGRDRAFT_56631; -.
DR   eggNOG; KOG2034; Eukaryota.
DR   InParanoid; D2UZK3; -.
DR   OMA; LFADWKK; -.
DR   OrthoDB; 22879at2759; -.
DR   Proteomes; UP000006671; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:UniProtKB-UniRule.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR   InterPro; IPR000547; Clathrin_H-chain/VPS_repeat.
DR   InterPro; IPR007810; Pep3_Vps18.
DR   PANTHER; PTHR23323; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN; 1.
DR   PANTHER; PTHR23323:SF26; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 18 HOMOLOG; 1.
DR   Pfam; PF00637; Clathrin; 1.
DR   Pfam; PF05131; Pep3_Vps18; 2.
DR   SMART; SM00299; CLH; 1.
DR   PROSITE; PS50236; CHCR; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006671};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          114..427
FT                   /note="Pep3/Vps18/deep orange beta-propeller"
FT                   /evidence="ECO:0000259|Pfam:PF05131"
FT   DOMAIN          501..598
FT                   /note="Pep3/Vps18/deep orange beta-propeller"
FT                   /evidence="ECO:0000259|Pfam:PF05131"
FT   REGION          35..100
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          860..885
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1067..1108
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1154..1181
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        35..75
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1250 AA;  142992 MW;  4497028A06C0ECD4 CRC64;
     MLPHDEEDLL NGGDWDVGLG GFSSRQTTNK KLGFSTTKDF TTAGDKTNSS SNLTNNKKTN
     DTSTLLSSAY NLNGIDSDED NDDENEGLAS SNKHDGETLP SDLLQQQNMG QDRFEVEEIK
     FEFSKSFTHV RASKGNLLLA TNQNTCIYVD DDFERYREFR LSHNDDDDDE KIHKCFIDPS
     GFHVLISMTN GDNYYFNTQY NKNPKLVAKL KNMIIESIGW DAEQCNREET GTILLGTNDS
     KIFECILYDD LKDPVKNSLK LLFDFNDCDM LVSTGPITGI EIEHFPKTKN SFNTYLVLVS
     TRLRMFEFIG GPTLQDVFAS YKQSFDLLKY KELPAKRSDM LPNSELHLFK KDSSSLTDQE
     SFAWLSNAGV YHGVLNFANP QSRQSGTSII TESEVIQYDN KSSSQVISIA ISEFHMFVLY
     PEKLQILMQP PGLCTASSVN PMMLSSLLVD PMNDNQTNQQ GIQGIDKFFG YGTTDNSNIT
     GSSNNLNLFM ASLTNVGEIS LSDIRVVYQK TFPVGTCGEL IGMCTDTSNR FIYLYSNSSV
     WRILIEDEER DVWKLYLEQA LDPKSSKESY FDVAFKLCKQ DPKTKDIVLS AKADYFFKVG
     RFNDAANIYA MTSKSFEQVS IAFHNKGQKD ALRIYVLAKL QSLKKNIKTE NQDATQLCCL
     CTWLTEMYLD KINELYDLVS LQSQQTRDIT SSNQVSFEEQ YTVIKNEFRK FLEDNKKYLN
     KETTFRLITS HGQTEEVLYY AMLIEDYERV ISHCITEKEY SEALEILNKF CTTRAYEDYF
     YKFSPILMQH LPKETVNTLT QKRFLDSGKL IPALMRYISH QQASMNNTGS LPPITLNSTF
     HTLTNNLNIT TALSSNNSML SSYTKKKSPE DDDEDALTES LDEDDDNAKI TQKLNENQQF
     SSLLTNDQQN HVIRYLEWCI KKQENEDPAI HNLLLTLYAD LDDDEKLLTF LDTEGENNFY
     DPKYALRVCS QKKKIEACVR LYSAMQLFDD AVDLALENDD IDLARECADK PDDDENRKKL
     WLKIAKHVIN HNTGVKQAIE FLSYTDKIKL EDILPYFPDF SRIDDFKEEI CKSLDQYKNE
     IEKLKNDMQL ATQTASEIRE DIKELKHRYG FITSNAKCDL SSKSVLTTDF YLFPCQHVFR
     ADALVEEVIK HTKSENGREK LKQLEEKRRL YNRQVELLNA NSSSGNQSSG SNSGLLDQKE
     LSQLQDELRE LDEILSSECP LCGEMMINSI DEGFIASDEN QSEILSWSIN
//
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