DLPC_DICDI
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 03-AUG-2022, entry version 90.
DE RecName: Full=Dynamin-like protein C;
DE EC=3.6.5.5;
GN Name=dlpC; ORFNames=DDB_G0271628;
OS Dictyostelium discoideum (Slime mold).
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 + H(+) + phosphate; 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 STRING; 44689.DDB0302372; -.
DR PaxDb; Q55AX0; -.
DR EnsemblProtists; EAL71678; EAL71678; DDB_G0271628.
DR GeneID; 8618029; -.
DR KEGG; ddi:DDB_G0271628; -.
DR dictyBase; DDB_G0271628; dlpC.
DR eggNOG; KOG0446; Eukaryota.
DR HOGENOM; CLU_320910_0_0_1; -.
DR InParanoid; Q55AX0; -.
DR OMA; ICYENDF; -.
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; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
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; -; 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; PTHR11566; 1.
DR Pfam; PF00350; Dynamin_N; 1.
DR PRINTS; PR00195; DYNAMIN.
DR SMART; SM00053; DYNc; 1.
DR SUPFAM; SSF52540; SSF52540; 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 53..92
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..221
FT /note="Polar residues"
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
