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Database: UniProt
Entry: A0A1E4RC23_9ASCO
LinkDB: A0A1E4RC23_9ASCO
Original site: A0A1E4RC23_9ASCO 
ID   A0A1E4RC23_9ASCO        Unreviewed;       689 AA.
AC   A0A1E4RC23;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Vacuolar sorting protein 1 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=HYPBUDRAFT_233045 {ECO:0000313|EMBL:ODV64786.1};
OS   Hyphopichia burtonii NRRL Y-1933.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Hyphopichia.
OX   NCBI_TaxID=984485 {ECO:0000313|EMBL:ODV64786.1, ECO:0000313|Proteomes:UP000095085};
RN   [1] {ECO:0000313|Proteomes:UP000095085}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL Y-1933 {ECO:0000313|Proteomes:UP000095085};
RG   DOE Joint Genome Institute;
RA   Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA   Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA   Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA   Klenk H.-P., Labutti K., Lapidus A., Lindquist E., Lipzen A.,
RA   Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA   Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA   Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V., Jeffries T.W.;
RT   "Comparative genomics of biotechnologically important yeasts.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC       superfamily. Dynamin/Fzo/YdjA family. {ECO:0000256|RuleBase:RU003932}.
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DR   EMBL; KV454546; ODV64786.1; -; Genomic_DNA.
DR   RefSeq; XP_020073853.1; XM_020223158.1.
DR   AlphaFoldDB; A0A1E4RC23; -.
DR   STRING; 984485.A0A1E4RC23; -.
DR   GeneID; 30997707; -.
DR   OrthoDB; 1052588at2759; -.
DR   Proteomes; UP000095085; Unassembled WGS sequence.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0006996; P:organelle organization; IEA:UniProt.
DR   CDD; cd08771; DLP_1; 1.
DR   Gene3D; 1.20.120.1240; Dynamin, middle domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR022812; Dynamin.
DR   InterPro; IPR001401; Dynamin_GTPase.
DR   InterPro; IPR019762; Dynamin_GTPase_CS.
DR   InterPro; IPR045063; Dynamin_N.
DR   InterPro; IPR000375; Dynamin_stalk.
DR   InterPro; IPR030381; G_DYNAMIN_dom.
DR   InterPro; IPR003130; GED.
DR   InterPro; IPR020850; GED_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR11566; DYNAMIN; 1.
DR   PANTHER; PTHR11566:SF220; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 1; 1.
DR   Pfam; PF01031; Dynamin_M; 1.
DR   Pfam; PF00350; Dynamin_N; 1.
DR   Pfam; PF02212; GED; 1.
DR   PRINTS; PR00195; DYNAMIN.
DR   SMART; SM00053; DYNc; 1.
DR   SMART; SM00302; GED; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00410; G_DYNAMIN_1; 1.
DR   PROSITE; PS51718; G_DYNAMIN_2; 1.
DR   PROSITE; PS51388; GED; 1.
PE   3: Inferred from homology;
KW   GTP-binding {ECO:0000256|RuleBase:RU003932};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU003932};
KW   Reference proteome {ECO:0000313|Proteomes:UP000095085}.
FT   DOMAIN          26..318
FT                   /note="Dynamin-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51718"
FT   DOMAIN          603..689
FT                   /note="GED"
FT                   /evidence="ECO:0000259|PROSITE:PS51388"
FT   REGION          80..100
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          536..566
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        548..566
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   689 AA;  76847 MW;  C5E6D30B1FE9B3B3 CRC64;
     MDETLIATIN KLQDALAPLG GGSASPVDLP QITVVGSQSS GKSSVLENIV GRDFLPRGTG
     IVTRRPLILQ LINKRSTPKS NGDLAGINTK NDKGEESENN ADEWGEFLHL PNKRIYNFEE
     IREEIVRETD AKTGKNLGIS ASPINLRIYS PHVLTLTLVD LPGLTKVPVG DQPKDIERQI
     REMIMKFISK PNAIILSVNA SNTDLANSDG LKLAREVDPE GSRTIGVLTK VDLMDHGTDV
     IDILAGRVIP LRFGYVPVIN RGQKDIEQKK TIREALKDES NYFENHPSYK AKAHFCGTPY
     LAKKLNGILL HHIKGTLPDI KMRIEHSLKK YQNELSLLGP EMSESPTSIA LNMITNFSKD
     YNGILNGEAR ELTSQELSGG ARISFVFHEI FKNGINALDP YDQIKDADIR TIMHNTSGSA
     PSLFVGTQAF EVLVKQQIHR MEEPSTRCIN LIFDELVRIL SQIISQTQYS RYPQLKEQLS
     NHFIQFLRDA LIPCNTFVTD IIKSEETYVN TAHPDLLKGS QAMAIVEEKF HPKPQVAVDP
     KTGKPLPPSQ QPVQQQSPKD DNSNGFFGGF FSSKNKKRLQ SMEAPPPVLR ATGTMTERET
     METEVIKLLI SSYFNIVKRT VADVVPKAIM LKLIVKSKED IQKELLEKLY NSPDLGDLVK
     ENELTVQKRK ECLKMVEVLR NASEIVSSV
//
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