ID A0A0G2H068_9PEZI Unreviewed; 697 AA.
AC A0A0G2H068;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 22-FEB-2023, entry version 30.
DE SubName: Full=Putative vacuolar dynamin-like gtpase {ECO:0000313|EMBL:KKY22235.1};
GN ORFNames=UCDDS831_g03794 {ECO:0000313|EMBL:KKY22235.1};
OS Diplodia seriata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Diplodia.
OX NCBI_TaxID=420778 {ECO:0000313|EMBL:KKY22235.1, ECO:0000313|Proteomes:UP000034182};
RN [1] {ECO:0000313|EMBL:KKY22235.1, ECO:0000313|Proteomes:UP000034182}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS831 {ECO:0000313|EMBL:KKY22235.1};
RA Morales-Cruz A., Amrine K.C., Cantu D.;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKY22235.1, ECO:0000313|Proteomes:UP000034182}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS831 {ECO:0000313|EMBL:KKY22235.1};
RA Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT "Distinctive expansion of gene families associated with plant cell wall
RT degradation and secondary metabolism in the genomes of grapevine trunk
RT pathogens.";
RL Submitted (MAY-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:KKY22235.1}.
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DR EMBL; LAQI01000078; KKY22235.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2H068; -.
DR Proteomes; UP000034182; 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}.
FT DOMAIN 34..323
FT /note="Dynamin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51718"
FT DOMAIN 610..697
FT /note="GED"
FT /evidence="ECO:0000259|PROSITE:PS51388"
FT REGION 537..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 697 AA; 77573 MW; 197A82E8ADE4AE42 CRC64;
MTANPTAINV NDPGLITLVN RLQDVFTTVG VQNPIDLPQI AVVGSQSSGK SSVLENIVGR
DFLPRGTGIV TRRPLILQLI NRASTSKTPN GTSETVEGTT DSQSNVDEWG EFLHIPGQKF
HDFNKIREEI VRETEAKTGR NAGISPAPIN LRIYSPNVLT LTLVDLPGLT KVPIGDQPRD
IERQIREMVL KQISKPNAII LAVTAANTDL ANSDGLKLAR EVDPEGQRTI GVLTKVDLMD
EGTDVVDILA GRIIPLRLGY VPVVNRGQRD IENKKPISYA LEHERQYFEN HKAYRNKSAY
CGTPYLARKL NLILMMHIKQ TLPDIKARIA SSLQKYSVEL AQLGDSILGN SSNIVLNMIT
EFSNEYRSVL EGNNQELSSI ELSGGARISF VYHELYSNGV KAVDPFDQVK DIDIRTVLYN
SSGSAPALFV GTTAFELIVK QQIKRLEDPS LKCVSLVYDE LIRILGQLLS KPMFRRYPAL
KEKFHAVAVH FFKKAMEPTN KLVKDLVAME ACYINTGHPD FINGSRAMAI VHERHNAAKP
TQVDPKTGKP LPPTAIPPRS ASPSIDGDNG SGFFGSFFAS KNKKKMAAME APPPQLKASG
TLSEKEAQEV EVIKLLISSY FNIVKRTMID MVPKAIMLTL VSFTKDEMQR EFLEMMYRTE
ELDDLLKESE YTVRRRKECQ QMVESLTRAQ EIVNQVQ
//