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DLPB_DICDI
ID   DLPB_DICDI              Reviewed;         808 AA.
AC   Q54MH8;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Dynamin-like protein B;
DE            EC=3.6.5.5;
GN   Name=dlpB; ORFNames=DDB_G0285931;
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=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   [2]
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 contains more than 2 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; AAFI02000082; EAL64500.1; -; Genomic_DNA.
DR   RefSeq; XP_638012.1; XM_632920.1.
DR   AlphaFoldDB; Q54MH8; -.
DR   SMR; Q54MH8; -.
DR   STRING; 44689.DDB0302371; -.
DR   PaxDb; Q54MH8; -.
DR   EnsemblProtists; EAL64500; EAL64500; DDB_G0285931.
DR   GeneID; 8625363; -.
DR   KEGG; ddi:DDB_G0285931; -.
DR   dictyBase; DDB_G0285931; dlpB.
DR   eggNOG; KOG0446; Eukaryota.
DR   HOGENOM; CLU_348987_0_0_1; -.
DR   InParanoid; Q54MH8; -.
DR   OMA; KAYNKIM; -.
DR   PhylomeDB; Q54MH8; -.
DR   BRENDA; 3.6.5.5; 1939.
DR   PRO; PR:Q54MH8; -.
DR   Proteomes; UP000002195; Chromosome 4.
DR   GO; GO:0032154; C:cleavage furrow; IDA:dictyBase.
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:0007015; P:actin filament organization; IGI:dictyBase.
DR   GO; GO:0061952; P:midbody abscission; IMP:dictyBase.
DR   GO; GO:0000281; P:mitotic cytokinesis; IMP:dictyBase.
DR   GO; GO:0006997; P:nucleus organization; IMP:dictyBase.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR022812; Dynamin.
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   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51718; G_DYNAMIN_2; 1.
PE   2: Evidence at transcript level;
KW   Cell cycle; Cell division; Cytoplasm; GTP-binding; Hydrolase;
KW   Motor protein; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..808
FT                   /note="Dynamin-like protein B"
FT                   /id="PRO_0000371338"
FT   DOMAIN          43..340
FT                   /note="Dynamin-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   REGION          53..60
FT                   /note="G1 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   REGION          79..80
FT                   /note="G2 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   REGION          150..153
FT                   /note="G3 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   REGION          239..242
FT                   /note="G4 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   REGION          276..279
FT                   /note="G5 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   REGION          536..565
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          665..695
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        541..565
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         53..60
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   BINDING         150..154
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   BINDING         239..242
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   808 AA;  92714 MW;  4F0410125AA5ED09 CRC64;
     MDRQSVVKST AIPFPLNFDN EKYDDMYKAY NKIMVLARDL NAFIETPEFV FIGKDGNGKS
     ALIESFIGFP MMIGEGSSLR PLHITLMNNA RCEEPIVTFK RDRSLDSYEF DRQIELSMVS
     SEISKRNQKT SIPIEITIEY RYYLNMLLIE PPSVSIQPTN AITIQGQSMT SPANQLANKI
     AKLSIGNEMG EMITQYTKSN NRTLVFVETS TNGGTNSSEM LELAKKLDYK LDRSIFVFNK
     FHSLLTGDQP FTNGRDANRF LGSPSIGAPT FFTTLPSTAQ RSQCNSKDQL SQLCDQLQQT
     DLNILEQLQF DKKYERNVGL SAFRHWISEF TWRKYLDSVP EVLKRLNSFR TTSEDQLYQI
     RQQLERTNAV TLRQIANSYV SIEFIQCIEK LVTRTLEGNP SLNGQTLEEE KSQDETGDWY
     DHNGKPILLL NDEKLVTFYD NKLYGGQQFE RLLTEFKCIT EVIQLEELSI SEVACAIGSN
     RPSNASVIAW AASDLAQKKI KEALLPLVDQ LFKRATYILR RLVDIVDRMI ENKKKSSFRR
     HGNSTSLFQD NSSPSSQSQS QSSSISQSAS LSSENMIYGI QSINGSDSVS RPSHENTIVN
     VEDHPYFIYS VKEMYFKYVD QIAADCKNKC MDEFYTTRLI YWDLQSNKDL KKFCTDSPCV
     SLNNSLNNNN KSTTPGNNNN NNNNNSNNNY NNSNHILNPK ETHTMVTELA SKLFQDIRNR
     MSKNIMLKCY NYFLIPMQMD LKLNIQDNIT KLSDAMLEEI FEIQTTKERL REDEQHLAQI
     CNQFIQQEEN YKKYSQSFSH PFPSAVRN
 
 
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