ID I7M2E9_TETTS Unreviewed; 771 AA.
AC I7M2E9;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Dynamin central region family protein {ECO:0000313|EMBL:EAS00259.2};
GN ORFNames=TTHERM_00218320 {ECO:0000313|EMBL:EAS00259.2};
OS Tetrahymena thermophila (strain SB210).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC Tetrahymena.
OX NCBI_TaxID=312017 {ECO:0000313|EMBL:EAS00259.2, ECO:0000313|Proteomes:UP000009168};
RN [1] {ECO:0000313|Proteomes:UP000009168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB210 {ECO:0000313|Proteomes:UP000009168};
RX PubMed=16933976; DOI=10.1371/journal.pbio.0040286;
RA Eisen J.A., Coyne R.S., Wu M., Wu D., Thiagarajan M., Wortman J.R.,
RA Badger J.H., Ren Q., Amedeo P., Jones K.M., Tallon L.J., Delcher A.L.,
RA Salzberg S.L., Silva J.C., Haas B.J., Majoros W.H., Farzad M.,
RA Carlton J.M., Smith R.K. Jr., Garg J., Pearlman R.E., Karrer K.M., Sun L.,
RA Manning G., Elde N.C., Turkewitz A.P., Asai D.J., Wilkes D.E., Wang Y.,
RA Cai H., Collins K., Stewart B.A., Lee S.R., Wilamowska K., Weinberg Z.,
RA Ruzzo W.L., Wloga D., Gaertig J., Frankel J., Tsao C.-C., Gorovsky M.A.,
RA Keeling P.J., Waller R.F., Patron N.J., Cherry J.M., Stover N.A.,
RA Krieger C.J., del Toro C., Ryder H.F., Williamson S.C., Barbeau R.A.,
RA Hamilton E.P., Orias E.;
RT "Macronuclear genome sequence of the ciliate Tetrahymena thermophila, a
RT model eukaryote.";
RL PLoS Biol. 4:1620-1642(2006).
CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC superfamily. Dynamin/Fzo/YdjA family. {ECO:0000256|RuleBase:RU003932}.
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DR EMBL; GG662621; EAS00259.2; -; Genomic_DNA.
DR RefSeq; XP_001020504.2; XM_001020504.3.
DR AlphaFoldDB; I7M2E9; -.
DR STRING; 312017.I7M2E9; -.
DR EnsemblProtists; EAS00259; EAS00259; TTHERM_00218320.
DR GeneID; 7838590; -.
DR KEGG; tet:TTHERM_00218320; -.
DR eggNOG; KOG0446; Eukaryota.
DR HOGENOM; CLU_008964_5_0_1; -.
DR InParanoid; I7M2E9; -.
DR OMA; IQRRKEC; -.
DR OrthoDB; 1052588at2759; -.
DR Proteomes; UP000009168; Unassembled WGS sequence.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR CDD; cd08771; DLP_1; 1.
DR Gene3D; 1.20.120.1240; Dynamin, middle domain; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; DYNAMIN; 1.
DR PANTHER; PTHR11566:SF21; DYNAMIN-1-LIKE PROTEIN; 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; P-loop containing nucleoside triphosphate hydrolases; 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 GTP-binding {ECO:0000256|RuleBase:RU003932};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU003932};
KW Reference proteome {ECO:0000313|Proteomes:UP000009168}.
FT DOMAIN 23..291
FT /note="Dynamin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51718"
FT DOMAIN 681..771
FT /note="GED"
FT /evidence="ECO:0000259|PROSITE:PS51388"
FT REGION 507..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..578
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 771 AA; 88488 MW; 8ADCA64BB7DBB222 CRC64;
MDKLIPLINE IHDVLSKSQL SNQLRLPQIV VIGSQSTGKS SLLESIVGQE ILPRGKGIVT
RRPIEIQLKN QQNAEQDYVE FSERRGEKIT DMDQVRKMID EDTEKIAGKN KAISNVPLRL
KFYSKNVVDL ILVDLPGMTK NPVGDQPQDI EQQILNLIEP YIKNPNSIIM AVSKGSDDLA
NSESLKLSRK IDPQGNRTIG VITQLDLIDE GADVLNDLQN KTYPLKLGYV GVIMRGQKDI
KIKSIKEQIA DEKAYFENHS IYKRVSNKMG IPYLIKLLNL SLMNHIKKTL PNIRENIVQM
LNDRENDLKQ YGDYSSLEDK KDRGIFVLRL ISQFTKSYNS LIQGHYIQTN NDELQGGSRI
QYIFNNIFRK SITELNPFDI LKDEDIRTAI KNADGLRQSL FVAEGAFENL VKQQISRLLN
PSIQCSHLVY EELRRIINLI NVPEIQRFDN FNNRIFQVME DVLERSLKPT DQMIKNLIEV
ELGYINTNHP DFIGGIELVQ NQSEQMCKEE EQKRNQQKPQ AAQYANKNER GQETDSDAKS
VISNKSQAIG GIERNQKRQQ SQNVQATSQS TPTDQDSSFW SWLPFSSKQN KQTELLDSKL
KIMNMKKLAE ENQGKDFSDS YSQNSPKGYT RRVYREFMAP QSYNDDYSIN NINQGYQGNL
PQVPTNIRLE DKPSKREMSE AEMIKNLIVS YFNIVKKNIN DSVPKTIVSF LVNRSVNIAE
RELVSNLYKE DIFDDLLAEN SYIAKQREET KAQMILLRSC LNVLNDLDAK F
//