DYNB_DICDI
ID DYNB_DICDI Reviewed; 920 AA.
AC Q9U1M9; Q54XV5;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Dynamin-B;
GN Name=dymB; ORFNames=DDB_G0277851;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=AX2;
RA Noethe H.B., Manstein D.J.;
RT "Functional characterization of Dictyostelium dynamin B.";
RL (In) Abstracts of the 39th Annual Meeting of American Society of Cell
RL Biology, abstract#1818, Washington DC (1999).
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).
CC -!- FUNCTION: Enzyme hydrolyzing GTP. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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; AJ251163; CAB64379.1; -; Genomic_DNA.
DR EMBL; AAFI02000023; EAL68098.1; -; Genomic_DNA.
DR RefSeq; XP_642447.1; XM_637355.1.
DR AlphaFoldDB; Q9U1M9; -.
DR SMR; Q9U1M9; -.
DR STRING; 44689.DDB0215390; -.
DR PaxDb; Q9U1M9; -.
DR EnsemblProtists; EAL68098; EAL68098; DDB_G0277851.
DR GeneID; 8621653; -.
DR KEGG; ddi:DDB_G0277851; -.
DR dictyBase; DDB_G0277851; dymB.
DR eggNOG; KOG0446; Eukaryota.
DR HOGENOM; CLU_008964_5_0_1; -.
DR InParanoid; Q9U1M9; -.
DR OMA; HGLTHCC; -.
DR PhylomeDB; Q9U1M9; -.
DR Reactome; R-DDI-1169408; ISG15 antiviral mechanism.
DR Reactome; R-DDI-169911; Regulation of Apoptosis.
DR Reactome; R-DDI-196025; Formation of annular gap junctions.
DR Reactome; R-DDI-8856828; Clathrin-mediated endocytosis.
DR PRO; PR:Q9U1M9; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0000331; C:contractile vacuole; IDA:dictyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:dictyBase.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:dictyBase.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:dictyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:dictyBase.
DR GO; GO:0031143; C:pseudopodium; IDA:dictyBase.
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:0098609; P:cell-cell adhesion; IMP:dictyBase.
DR GO; GO:0031589; P:cell-substrate adhesion; IMP:dictyBase.
DR GO; GO:0071476; P:cellular hypotonic response; IMP:dictyBase.
DR GO; GO:0060151; P:peroxisome localization; IMP:dictyBase.
DR GO; GO:0006909; P:phagocytosis; IMP:dictyBase.
DR GO; GO:0009617; P:response to bacterium; HEP: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; 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; PTHR11566; 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; SSF52540; 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 Coiled coil; Cytoplasm; GTP-binding; Hydrolase; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..920
FT /note="Dynamin-B"
FT /id="PRO_0000384412"
FT DOMAIN 154..448
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT DOMAIN 825..916
FT /note="GED"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00720"
FT REGION 65..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..171
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 190..192
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 204..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..293
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 359..362
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 389..392
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 680..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 724..751
FT /evidence="ECO:0000255"
FT COMPBIAS 212..232
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..763
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 776..790
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 164..172
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O00429"
FT BINDING 359..365
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O00429"
FT BINDING 390..393
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O00429"
SQ SEQUENCE 920 AA; 105254 MW; 25E1D3B7A2EA0A15 CRC64;
MLSSTAILKA SGDVAINYQQ YIYPIIINKL STLNYTIKNK KYYSQYKYSI QFQNEFQKNL
KIYNNSNNNN NNNNNNKINK NNNNNNNNIS KFFIQNNNID KKVLRHFYSS TKLNYAKQQQ
QLFKNNETFN ETVGASLLPI INKLQENAAL IGSEITLPQI IVVGSQSSGK SSVLENLVGR
DFLPRGSGLV TRRPLVLQLY QTTTTSRNNV NENEDEDEDD NYYDNDNDDN SLEEWGEFGH
TGTNRFNFQE IKEEIERETE RIAGPNKDIS SEPIVLKIYS PKVVPLTLVD LPGLTRVAIE
DQPPDIEEKI KSMIIDYISN PNSIILAITP ANQDIVTSDA LKLAQQVDPL GKRTIGVLTK
LDLMDKGTDA IDILLGNSIP LSLGFVGVVN RSQQDINNRK PIEQMLADEW KWFDQHPVYH
RITNQLGTKY LAQKCNKILT KHIRDTFPSV KNQIRQLIKK YESDLEKYGE PIPLRSAEKS
RLLLDILNEF SRKYRADLDG TNEELILNEF NGGARIRYIF SKAFQSTTAA AATTSTDNSG
GGEPFGWLSD QQLKIALRNS GSTMFIPQKI FDSLIRKQLE RVREPLIQTS EIILDELIRI
LTQADYSHVL SRFPILKERI VEVSNNALRK LVKECNQSIS QMVDAEMSFI NTNHPNYLYQ
LNNLLFSSSS SSFVVPQGAF QSTSSTSSSP TSSSSSLPLP QNSNPYNDAL NPYNIDRSYP
IDNQIKQQQQ QQQQQQQQSY QQQQQQQQKQ QSGFLSRIFG SSSSPPSPPS PPQPKQQQSH
EIQIQQQQQQ QQQQHLKKQN LIFDDKFKLE QYGLNDITED EKKQIYLLRR LLLAYNDIAQ
FNLQQNTMKL VSLLLIDKSK DILQKELIDS LYDQSSVDQL LRENELVVAK RNECIYKLDL
LKKAKKSLSQ SENSDLLHLY
