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
//