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Database: UniProt
Entry: A0A072P4P2_9EURO
LinkDB: A0A072P4P2_9EURO
Original site: A0A072P4P2_9EURO 
ID   A0A072P4P2_9EURO        Unreviewed;       707 AA.
AC   A0A072P4P2;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   22-FEB-2023, entry version 37.
DE   SubName: Full=Vacuolar protein sorting-associated protein 1 {ECO:0000313|EMBL:KEF54682.1};
GN   ORFNames=A1O9_09124 {ECO:0000313|EMBL:KEF54682.1};
OS   Exophiala aquamarina CBS 119918.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=1182545 {ECO:0000313|EMBL:KEF54682.1, ECO:0000313|Proteomes:UP000027920};
RN   [1] {ECO:0000313|EMBL:KEF54682.1, ECO:0000313|Proteomes:UP000027920}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 119918 {ECO:0000313|EMBL:KEF54682.1,
RC   ECO:0000313|Proteomes:UP000027920};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala aquamarina CBS 119918.";
RL   Submitted (MAR-2013) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KEF54682.1}.
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DR   EMBL; AMGV01000009; KEF54682.1; -; Genomic_DNA.
DR   RefSeq; XP_013257272.1; XM_013401818.1.
DR   AlphaFoldDB; A0A072P4P2; -.
DR   STRING; 1182545.A0A072P4P2; -.
DR   GeneID; 25284034; -.
DR   VEuPathDB; FungiDB:A1O9_09124; -.
DR   HOGENOM; CLU_008964_5_2_1; -.
DR   OrthoDB; 1052588at2759; -.
DR   Proteomes; UP000027920; 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:UP000027920}.
FT   DOMAIN          38..329
FT                   /note="Dynamin-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51718"
FT   DOMAIN          620..707
FT                   /note="GED"
FT                   /evidence="ECO:0000259|PROSITE:PS51388"
FT   REGION          545..579
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        554..568
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   707 AA;  78342 MW;  BCF243511A68295A CRC64;
     MAAAPAGGGH SINVNDPTLI ALVNKLQDVF TTVGVANPID LPQIVVVGSQ SSGKSSVLEN
     IVGRDFLPRG AGIVTRRPLV LQLIHRPIPA KLQTNGVSDK DLQNSTDSQA NVDEWGEFLH
     LPGQKFYDFN KIRDEIVKET EAKAGRNVGI SPAPINLRIY SPNVLTLTLV DLPGLTKVPV
     GDQPRDIERQ IKDMVLKQIS KPNAIILAVT AANVDLANSD GLKLAREVDP EGQRTIGVLT
     KIDLMDTGTD VVDILAGRII PLRLGYVPVV NRGQRDIENK KQIGLALKAE KEFFENHPSY
     RNKASYCGTP YLARKLNLIL MMHIKQTLPD IKTRIATSLQ KYSQELEQLG AGDLLGNNSS
     NIILNIITEF ANEYRTVLDG NSSELSSNEL SGGARISFVY HELYSNGIKA IDPFEQVKDI
     DIRTILYNSS GSSPALFVGT TAFELIVKQQ IRRLEEPSLK CVSLVYDELV RILGQLLQKQ
     LFRRYPGLKE RFHGVVIGFF RKAMDPTNKL VRDLVAMEAC YINTGHPDFL NGHRAMAIVN
     DRHNSAKPTQ VDPKTGKPLP PSVPPRAGSP SLPTDGSDQN SGFFGSFFAS KNKKKMAAME
     PPPATLKASG TLSERENQEV EVIKLLINSY FNITRRTMID MVPKAIMLSL VQYTKDEMQR
     ELLEHMYKTT ELDELLKESD YTVRRRKECQ QMVESLGKAS EIVSQVQ
//
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