FTSZA_DICDI
ID FTSZA_DICDI Reviewed; 517 AA.
AC Q54Z54; Q86AW4; Q9GPZ8;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Mitochondrial division protein fszA;
GN Name=fszA; Synonyms=ftsZA; ORFNames=DDB_G0277721;
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], AND SUBCELLULAR LOCATION.
RX PubMed=14665465; DOI=10.1128/ec.2.6.1315-1326.2003;
RA Gilson P.R., Yu X.-C., Hereld D., Barth C., Savage A., Kiefel B.R., Lay S.,
RA Fisher P.R., Margolin W., Beech P.L.;
RT "Two Dictyostelium orthologs of the prokaryotic cell division protein FtsZ
RT localize to mitochondria and are required for the maintenance of normal
RT mitochondrial morphology.";
RL Eukaryot. Cell 2:1315-1326(2003).
RN [2]
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 [3]
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: Probably involved in mitochondrion division process. When
CC overexpressed, induces mitochondrial tubule formation. Binds to and
CC hydrolyzes GTP (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000305|PubMed:14665465}.
CC -!- SIMILARITY: Belongs to the FtsZ family. {ECO:0000305}.
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DR EMBL; AF304356; AAG37880.1; -; Genomic_DNA.
DR EMBL; AAFI02000022; EAL68534.1; -; Genomic_DNA.
DR RefSeq; XP_642499.1; XM_637407.1.
DR AlphaFoldDB; Q54Z54; -.
DR SMR; Q54Z54; -.
DR STRING; 44689.DDB0219983; -.
DR PaxDb; Q54Z54; -.
DR EnsemblProtists; EAL68534; EAL68534; DDB_G0277721.
DR GeneID; 8621210; -.
DR KEGG; ddi:DDB_G0277721; -.
DR dictyBase; DDB_G0277721; fszA.
DR eggNOG; ENOG502QRFN; Eukaryota.
DR HOGENOM; CLU_024865_5_2_1; -.
DR InParanoid; Q54Z54; -.
DR OMA; SIMCNSG; -.
DR PhylomeDB; Q54Z54; -.
DR PRO; PR:Q54Z54; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:dictyBase.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IBA:GO_Central.
DR GO; GO:0007005; P:mitochondrion organization; IMP:dictyBase.
DR GO; GO:0048285; P:organelle fission; IBA:GO_Central.
DR CDD; cd02201; FtsZ_type1; 1.
DR Gene3D; 3.30.1330.20; -; 1.
DR Gene3D; 3.40.50.1440; -; 1.
DR HAMAP; MF_00909; FtsZ; 1.
DR InterPro; IPR000158; Cell_div_FtsZ.
DR InterPro; IPR020805; Cell_div_FtsZ_CS.
DR InterPro; IPR045061; FtsZ/CetZ.
DR InterPro; IPR024757; FtsZ_C.
DR InterPro; IPR008280; Tub_FtsZ_C.
DR InterPro; IPR037103; Tubulin/FtsZ-like_C.
DR InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom.
DR InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf.
DR InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR PANTHER; PTHR30314; PTHR30314; 1.
DR Pfam; PF12327; FtsZ_C; 1.
DR Pfam; PF00091; Tubulin; 1.
DR PRINTS; PR00423; CELLDVISFTSZ.
DR SMART; SM00864; Tubulin; 1.
DR SMART; SM00865; Tubulin_C; 1.
DR SUPFAM; SSF52490; SSF52490; 1.
DR SUPFAM; SSF55307; SSF55307; 1.
DR TIGRFAMs; TIGR00065; ftsZ; 1.
DR PROSITE; PS01134; FTSZ_1; 1.
PE 3: Inferred from homology;
KW GTP-binding; Mitochondrion; Nucleotide-binding; Reference proteome.
FT CHAIN 1..517
FT /note="Mitochondrial division protein fszA"
FT /id="PRO_0000327692"
FT REGION 496..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 60..64
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P0A029"
FT BINDING 147..149
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P0A029"
FT BINDING 178
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P0A029"
FT BINDING 182
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P0A029"
FT BINDING 225
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P0A029"
FT CONFLICT 105
FT /note="T -> P (in Ref. 1; AAG37880)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 517 AA; 56665 MW; F5488D5103AFE831 CRC64;
MSQFMIRYQI INLSKVFNSP KSLNFIKRYT TSTASTTTTT TNDDSNWIST PNITVCGIGG
GGCNSVNNMI NKELYGIDFV VANTDAQALA ISCSRKMVQL GKTLTRGLGA GAVPEVGKKA
TEESIEELMN QIGDTQMLFV TAGMGGGTGT GGAAVIASAA KAKGILTVGI VTKPFHFEGK
HRMKLAEQGL IELEKSVDSL IVIPNEKLME QSQELYIGNA FQMVDDVLYN SIRGISDILV
KPGLINLDFA DVRSIMCNSG KALMGVGEGE GKGRDAIAAN IALNNPLLEN INISGAKGVL
LNIAGSDLKL QEVDHIVSLV SSKVDPSANI IFGSTFDQQL EGKIRVTLIV TGMDQLIQQQ
QQQQKQTKIE SQVEQKLHST TIVDQELKPI EPQKSIIIEE EQEEQQQPKP IIPGIFVEQE
LLTTTTTANI TPSQQKQESL TQNNIFSPPQ QQQQQPSINL QPNYQQLYQQ LYQQQQQQLQ
QQQPISFLKR LSNLFFTNGN NNKPYNNNKN TPGSNYE
