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
//