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Database: UniProt
Entry: A0A1V6Q9S5_9EURO
LinkDB: A0A1V6Q9S5_9EURO
Original site: A0A1V6Q9S5_9EURO 
ID   A0A1V6Q9S5_9EURO        Unreviewed;       914 AA.
AC   A0A1V6Q9S5;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Dynamin-type G domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PENANT_c009G04381 {ECO:0000313|EMBL:OQD85732.1};
OS   Penicillium antarcticum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=416450 {ECO:0000313|EMBL:OQD85732.1, ECO:0000313|Proteomes:UP000191672};
RN   [1] {ECO:0000313|Proteomes:UP000191672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 31811 {ECO:0000313|Proteomes:UP000191672};
RX   PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA   Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA   Frisvad J.C., Workman M., Nielsen J.;
RT   "Global analysis of biosynthetic gene clusters reveals vast potential of
RT   secondary metabolite production in Penicillium species.";
RL   Nat. Microbiol. 2:17044-17044(2017).
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:OQD85732.1}.
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DR   EMBL; MDYN01000009; OQD85732.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6Q9S5; -.
DR   STRING; 416450.A0A1V6Q9S5; -.
DR   OrthoDB; 1052588at2759; -.
DR   Proteomes; UP000191672; 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; 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; IPR020850; GED_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR11566; DYNAMIN; 1.
DR   PANTHER; PTHR11566:SF237; INTERFERON-INDUCED GTP-BINDING PROTEIN MX; 1.
DR   Pfam; PF01031; Dynamin_M; 1.
DR   Pfam; PF00350; Dynamin_N; 1.
DR   PRINTS; PR00195; DYNAMIN.
DR   SMART; SM00053; DYNc; 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:UP000191672}.
FT   DOMAIN          235..508
FT                   /note="Dynamin-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51718"
FT   DOMAIN          800..893
FT                   /note="GED"
FT                   /evidence="ECO:0000259|PROSITE:PS51388"
FT   REGION          159..183
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          891..914
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        891..906
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   914 AA;  101354 MW;  6C20CE3C93331928 CRC64;
     MSGRILSHRL GPLLRNGHLA RHIHNAGSRT GGLLRADGGA ALRGRAWPIG ANAIHNIPAV
     RSISFARMLP KLALKLVRVP AMFGGATIAG LAYFQYQATQ AGNYAMDVFK QASETAGNTA
     STLFQGLQDV ADQTQRGWNK TTEDLDLPEW LQKILRLDEE SQKGESGGAD KEPKQSRAGT
     AAAAAATTSA FGYDKSEEED VRPARDAAED DQMMLLTRKM IEIRNILQTI GQSDTLTLPS
     IVVIGSQSSG KSSVLEAIVG HEFLPKGSNM VTRRPIELTL VNTPNAQSEY GEFPALGLGK
     ITDFTQIQRT LTDLNLAVPE KDCVTDDPIQ LTIYSPNVPD LSMIDLPGYI QVAGHDQPPE
     LKQKINDLCD KYIQPPNVIL AISAADVDLA NSTALRASRR VDPRGERTIG VITKMDLVSP
     ERGHDVLSDK KYPLRLGYVG VVSRIPQTNA LFSRGSGNIT SAILKNEHAY FSAHPGEFGP
     HSDVSVGVST LRKTLMHVLE QTMASSLSGT RDAISQELEE ATYEFKVQYN DRPLSAESHL
     AESLDSFKHS FKAFAESFGR PQVREMLKAE LDQRVMDILA QRYWNKPVED LDPPMLELDS
     LKDLPKSDPE SLYWHRKLDA STSSLTKLGI GRLATTVVAN ALHNHVDQLL SSSTFASHPG
     AHKQITDACN TILNDRFFST SDQVENCIKP YKFEIEVEDP EWAKGRDNVG RVLKDELKHC
     EQAMKHVEDV VGKRKLKDVV SFIDRVRKGD VVLEGNGEGG AGGFSAALLE RGREGLFLRD
     RADLIKMRLL AVRSKQCATQ KNKYYCPEVF LDVVADKLTS TAVLFLNVEL LSEFYYNFPR
     ELDTRLGRHL SDAEVERFAR EDPRIRRHLD IIRKKELLEL ALQKIESVRQ LDGRSRAPER
     PPPGKETRSR WGLF
//
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