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Database: UniProt
Entry: A0A139IQW6_9PEZI
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ID   A0A139IQW6_9PEZI        Unreviewed;       688 AA.
AC   A0A139IQW6;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   13-SEP-2023, entry version 28.
DE   RecName: Full=Vacuolar protein sorting-associated protein 1 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AC579_7410 {ECO:0000313|EMBL:KXT17002.1};
OS   Pseudocercospora musae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX   NCBI_TaxID=113226 {ECO:0000313|EMBL:KXT17002.1, ECO:0000313|Proteomes:UP000073492};
RN   [1] {ECO:0000313|EMBL:KXT17002.1, ECO:0000313|Proteomes:UP000073492}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 116634 {ECO:0000313|EMBL:KXT17002.1,
RC   ECO:0000313|Proteomes:UP000073492};
RA   Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT   "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT   link between parallel evolutionary changes in Pseudocercospora fijiensis
RT   and Pseudocercospora eumusae and increased virulence on the banana host.";
RL   Submitted (JUL-2015) 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:KXT17002.1}.
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DR   EMBL; LFZO01000027; KXT17002.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A139IQW6; -.
DR   Proteomes; UP000073492; 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:UP000073492}.
FT   DOMAIN          22..313
FT                   /note="Dynamin-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51718"
FT   DOMAIN          601..688
FT                   /note="GED"
FT                   /evidence="ECO:0000259|PROSITE:PS51388"
FT   REGION          69..93
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          527..556
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   688 AA;  76913 MW;  B28D698DB811A588 CRC64;
     MLQLARNREF DTLKHMAQVQ NPIDLPQIAV VGSQSSGKSS VLENIVGRDF LPRGTGIVTR
     RPLILQLINR SSTAKPQENG VPNGEKAENT DKEANSEEWG EFLHIPGQKF YDFNKIRDEI
     VKETESKTGR NAGISPAPIN LRIYSPNVLT LTLVDLPGLT KVPVGDQPRD IERQIREMVL
     KQISKPNAII LAVTAANTDL ANSDGLKLAR EVDPEGQRTI GVLTKVDLMD EGTDVVDILA
     GRIIPLRLGY VPVVNRGQRD IETKKAISYA LENEKNFFEN HKAYRNKASY CGTPYLARKL
     NLILMMHIKQ TLPDIKARIQ ASLQKYSAEL QSLGDSMLGN PANIILNIIT EFSNEYRTVL
     EGHSAELSSI ELSGGARIAF VYHELYSNGV KAVDPFDQVK DIDIRTILYN SSGSSPALFV
     GTTAFELIVK QQIKRLEDPS LKCVSLIYDE LIRILGQLVN KPMFRRYPAL KEKLHAVVVG
     FFKKAMDPTN KLVKDLVAME SCYVNTGHPD FINGHRAMAI VNEKHNASKP VQVDPKTGKP
     LPPSAQPPRA ATPSLDLDGE QSGFFGSFFA SKNKKKMAAM EPPPPTLKAS GTLSEKETQE
     VEVIKLLITS YFNIVRRTMI DMVPKAIMLN LVEHTKEEMQ RELLEQMYRT QELDDLLKES
     DYTIRRRKEC QQMVESLSRA AEIVSQVQ
//
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