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Database: UniProt
Entry: A0A317VZC3_9EURO
LinkDB: A0A317VZC3_9EURO
Original site: A0A317VZC3_9EURO 
ID   A0A317VZC3_9EURO        Unreviewed;       904 AA.
AC   A0A317VZC3;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Putative dynamin GTPase {ECO:0000313|EMBL:PWY78288.1};
GN   ORFNames=BO70DRAFT_363176 {ECO:0000313|EMBL:PWY78288.1};
OS   Aspergillus heteromorphus CBS 117.55.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1448321 {ECO:0000313|EMBL:PWY78288.1, ECO:0000313|Proteomes:UP000247233};
RN   [1] {ECO:0000313|EMBL:PWY78288.1, ECO:0000313|Proteomes:UP000247233}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 117.55 {ECO:0000313|EMBL:PWY78288.1,
RC   ECO:0000313|Proteomes:UP000247233};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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:PWY78288.1}.
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DR   EMBL; MSFL01000017; PWY78288.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A317VZC3; -.
DR   STRING; 1448321.A0A317VZC3; -.
DR   VEuPathDB; FungiDB:BO70DRAFT_363176; -.
DR   OrthoDB; 5350357at2759; -.
DR   Proteomes; UP000247233; Unassembled WGS sequence.
DR   GO; GO:0005525; F:GTP binding; IEA:InterPro.
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; 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:SF131; GTPASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G07630)-RELATED; 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   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51718; G_DYNAMIN_2; 1.
DR   PROSITE; PS51388; GED; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000247233}.
FT   DOMAIN          132..454
FT                   /note="Dynamin-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51718"
FT   DOMAIN          777..873
FT                   /note="GED"
FT                   /evidence="ECO:0000259|PROSITE:PS51388"
FT   REGION          1..93
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          552..587
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..55
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        58..77
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        78..93
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   904 AA;  103095 MW;  A364C12493517AF6 CRC64;
     MAALQSPVPP PPSPLIPAAT LEIGPSPAAN RRFIYPQQVN THQQETASHQ EIPLPQENTY
     RLEKRPRQEK SPQEDDIPQP ENTRANTVES TTTVMSRQAL REIDSINLIA GNMKELVKRI
     QDLRHIGIED NNIDLPKICV IGDQSAGKSS LIEGMSEIKV PRCAGTCTRC PMEINLSESE
     PGQSWTCKVF LSRRYMYDES VKFNKVSQKS RSLGPWHEQD QEDEPFITLT NKKDVQEAIR
     WAQIAILNPK TPSSLYTPGQ NSLADSSWQV KFSPNIVRLD ITAPGFPNLS FYDLPGVISQ
     AEQEDERYLV TLVENLVREY IAQPNCIVLL TLPMTNDATN SGAARIMQEV KGAKERTLGV
     LTKPDRVQAG ESHAQWVEIL QGGKFSLGYG YYVVRNNPDP EVEHAQAREE EETFFASDPW
     VGNGLAVYED KFGTRRLQAA LSTLLLEQIQ GCLPRIIEQI NKKADRIDSE LQTLPDPPTA
     NVQYILCRKL NEFKDHIRAH VNGGSSQYPL QKIWVHIASD FKRALAKTRP TVRLLSPEDR
     IFYTTIPDCE GGSDSDCEMT SAPQPVKRKS PENPRNVPTP PEATADQHEG YYTEPFKKFQ
     KSPLMFTWET IREINEDSYR AGLPDQTDPK AIEIMNQMSV KHWCDPLGVF LNSTYRLVRD
     MLLKQLNEVF AQFHQTGLYR ELKRIIIQYL RDLRAEHFEH AQENFNIEYN KPFTMATSAL
     DLATKSAHQY LSSQRQTLRA GLYLDTKGKF PRGDARREAE LRKLSATDIG PDRFAQELKM
     MANTRAYYDM ASSRFVDSIC QGVHTKLFAK CREELISVIE SELRIFDDNA LDRCLELMTE
     DPERQRRRLQ LLKEREKITK AQEWLNSAKK EDEFADTLVD DKVRIKSQPP DEWTSYTVST
     NGLE
//
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