ID   DLPC_DICDI              Reviewed;         904 AA.
AC   Q55AX0; Q86JH7;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 2.
DT   02-SEP-2026, entry version 106.
DE   RecName: Full=Dynamin-like protein C;
DE            EC=3.6.5.5;
GN   Name=dlpC; ORFNames=DDB_G0271628;
OS   Dictyostelium discoideum (Social amoeba).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=12097910; DOI=10.1038/nature00847;
RA   Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA   Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA   Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA   Noegel A.A.;
RT   "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL   Nature 418:79-85(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
RN   [3]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX   PubMed=18809930; DOI=10.1073/pnas.0802412105;
RA   Miyagishima S.Y., Kuwayama H., Urushihara H., Nakanishi H.;
RT   "Evolutionary linkage between eukaryotic cytokinesis and chloroplast
RT   division by dynamin proteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:15202-15207(2008).
CC   -!- FUNCTION: Involved in cytokinesis. May hydrolyze GTP.
CC       {ECO:0000269|PubMed:18809930}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + phosphate + H(+); Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.5;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- DEVELOPMENTAL STAGE: Expression begins during cell cycle progression,
CC       between 12 and 24 hours after germination. Reach a maximum around mid-
CC       log phase and disappear during the stationary phase.
CC       {ECO:0000269|PubMed:18809930}.
CC   -!- DISRUPTION PHENOTYPE: Produced cells are larger and a large amount of
CC       them contained more than two nuclei. {ECO:0000269|PubMed:18809930}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC       superfamily. Dynamin/Fzo/YdjA family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01055}.
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DR   EMBL; AAFI02000006; EAL71678.2; -; Genomic_DNA.
DR   RefSeq; XP_645576.2; XM_640484.2.
DR   AlphaFoldDB; Q55AX0; -.
DR   FunCoup; Q55AX0; 1.
DR   STRING; 44689.Q55AX0; -.
DR   PaxDb; 44689-Q55AX0; -.
DR   GeneID; 8618029; -.
DR   KEGG; ddi:DDB_G0271628; -.
DR   dictyBase; DDB_G0271628; dlpC.
DR   VEuPathDB; AmoebaDB:DDB_G0271628; -.
DR   eggNOG; KOG0446; Eukaryota.
DR   HOGENOM; CLU_320910_0_0_1; -.
DR   InParanoid; Q55AX0; -.
DR   OMA; MALKMHE; -.
DR   PhylomeDB; Q55AX0; -.
DR   BRENDA; 3.6.5.5; 1939.
DR   PRO; PR:Q55AX0; -.
DR   Proteomes; UP000002195; Chromosome 2.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR   GO; GO:0000281; P:mitotic cytokinesis; IMP:dictyBase.
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; IPR045063; Dynamin_N.
DR   InterPro; IPR030381; G_DYNAMIN_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR11566; DYNAMIN; 1.
DR   PANTHER; PTHR11566:SF169; DYNAMIN-LIKE PROTEIN C; 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; PS51718; G_DYNAMIN_2; 1.
PE   2: Evidence at transcript level;
KW   Cell cycle; Cell division; Coiled coil; Cytoplasm; GTP-binding; Hydrolase;
KW   Motor protein; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..904
FT                   /note="Dynamin-like protein C"
FT                   /id="PRO_0000371339"
FT   DOMAIN          119..441
FT                   /note="Dynamin-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   REGION          53..93
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          129..136
FT                   /note="G1 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   REGION          155..157
FT                   /note="G2 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   REGION          169..227
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          278..281
FT                   /note="G3 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   REGION          343..346
FT                   /note="G4 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   REGION          378..381
FT                   /note="G5 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   REGION          821..840
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          853..904
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          44..102
FT                   /evidence="ECO:0000255"
FT   COILED          781..811
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        67..90
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        183..213
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        853..876
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        877..891
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         129..136
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   BINDING         278..282
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   BINDING         343..346
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   904 AA;  104370 MW;  F6C3DA0FA08C7288 CRC64;
     MSHQQQQAHF DISSNSTLTT NTIATTTNAS VSSSPQLNKA QMAIAEAMAL KMHEEEKKKR
     EEKKRKRDNE ELLSKQVRTK LENERKKLDD SESINASTNQ ELYSLFNDLQ MISHDHNISF
     DTPELVVVGM QSDGKSSFIE SLLGFQFNIV ETNIGTRRPL IIQMINNPSK QQPSCRFKKE
     DYSNSYGGSS SSTSTTSGNS NHNTDKQQNV SSSQGGGGGS NNLNEDKWEE YETPVNELTE
     EIIRRTNERT GRAGDRVSSI PIFLRVEFAH CSNLNIYDTP GFRKGGDERL KYEISEMVKK
     LIEPKNRIIV CLEQSNVEWA NTISRPLVKK IDPDFSRTIL VNTKFDNRVK ELRNRESAHK
     YLEGEGIIAQ KKPFFISLPL KRNLETHRFK DAMKETFLDD YRKLLEIGFD ENRFGGQIGI
     YKVRQYVENL LHEKYQQNLL PSMLQLESIC KKTEADIVRV KKELSDNNIV TLKEKVMRFV
     SNFNGQIERL LEGSVVGDPD EFGQTLLQEK ENCSVQPWPG YNFDFDIQNS NYSLYGGAQY
     ERLLNEFEFV IHSKEFPETS INEVASAIGV SKSHNSPIYE LAATNIFQTK SKKVLLPLID
     IVLQRSSYIM KRLFDISVSI LGKDENESSH TVSLYEHFLK ELQSQYEKFI QTIESECKSR
     LKDDFEMFTK IVDWNLLSGL TEIKPYNYLK VSPEETKQRV ISIMDCKKLE DEPLSRSRNI
     DDDTYQKVCM IAGRLFSGIR FFFSKLIRNK LNAFFLDPMF QKLGSFVTDY FSKLNDQKYE
     EMFQLGLKEL ENKLHKLEFQ LIDCKKNRDK FKDVYNRMKQ SLNQNQNQNS SSSSNSASSS
     NNNVIIKHQQ SLNGKFSTPD KNSLTMSPFT SPFTQSNYHQ HNNNNYQINQ QPLDINNDHY
     FDQN
//