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Database: UniProt
Entry: A0A176VW38_MARPO
LinkDB: A0A176VW38_MARPO
Original site: A0A176VW38_MARPO 
ID   A0A176VW38_MARPO        Unreviewed;       424 AA.
AC   A0A176VW38;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Dynamin-type G domain-containing protein {ECO:0000259|PROSITE:PS51718};
GN   ORFNames=AXG93_2415s1630 {ECO:0000313|EMBL:OAE24581.1};
OS   Marchantia polymorpha subsp. ruderalis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC   Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX   NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE24581.1, ECO:0000313|Proteomes:UP000077202};
RN   [1] {ECO:0000313|EMBL:OAE24581.1, ECO:0000313|Proteomes:UP000077202}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Tak-1 and cv. Tak-2 {ECO:0000313|Proteomes:UP000077202};
RC   TISSUE=Whole gametophyte {ECO:0000313|EMBL:OAE24581.1};
RA   Honkanen S., Jones V.A., Morieri G., Champion C., Hetherington A.J.,
RA   Kelly S., Saint-Marcoux D., Proust H., Prescott H., Dolan L.;
RT   "Mechanisms controlling the formation of the plant cell surface in tip-
RT   growing cells are functionally conserved among land plants.";
RL   Submitted (MAR-2016) 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:OAE24581.1}.
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DR   EMBL; LVLJ01002571; OAE24581.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A176VW38; -.
DR   OrthoDB; 447862at2759; -.
DR   Proteomes; UP000077202; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
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; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR11566; DYNAMIN; 1.
DR   PANTHER; PTHR11566:SF21; DYNAMIN-1-LIKE PROTEIN; 1.
DR   Pfam; PF01031; Dynamin_M; 2.
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.
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:UP000077202}.
FT   DOMAIN          59..333
FT                   /note="Dynamin-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51718"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   424 AA;  46376 MW;  F77B86BA46B3CA03 CRC64;
     MAQPQANPVM PSAPASPSAA VPPALPPSPS PPAVYLGQSV IPLVNKLQDI FSQLGSASTI
     DLPQVAVVGS QSSGKSSVLE AMVGRDFLPR GADICTRRPL VLQLVQTVRR PEDRSELVEW
     GEFLHIPGRR FTDFTAIRKE IQAETDRELG TNKGISEKQI RLKIFSPNVL NITLVDLPGI
     TKVPVGDQPS DIEARVRTMI LNYIKHETCI ILAVSPANAD LANSDALQMA RIADPDGSRT
     IGVITKLDIM DRGTDARNFL LGNVVPLRLG YIGVVNRSQE DIQANKTIRE ALGYEENFFR
     SRPILVQHIR AILPDLKARI STQMVTLQKE LAGYGELTDS KSGQGALLLN IITKYSQDVV
     VNYTTPLCER IRPVASKISQ RQIMNSGFVF YTTQCAISGL VSHLGLLFDK EVDSHTLPDL
     QPFA
//
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