ID   A0A0N5A7N0_9BILA        Unreviewed;       820 AA.
AC   A0A0N5A7N0;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=dynamin GTPase {ECO:0000256|ARBA:ARBA00011980};
DE            EC=3.6.5.5 {ECO:0000256|ARBA:ARBA00011980};
OS   Syphacia muris.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Oxyuridomorpha; Oxyuroidea; Oxyuridae; Syphacia.
OX   NCBI_TaxID=451379 {ECO:0000313|Proteomes:UP000046393, ECO:0000313|WBParaSite:SMUV_0000003601-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:SMUV_0000003601-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
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   AlphaFoldDB; A0A0N5A7N0; -.
DR   STRING; 451379.A0A0N5A7N0; -.
DR   WBParaSite; SMUV_0000003601-mRNA-1; SMUV_0000003601-mRNA-1; SMUV_0000003601.
DR   Proteomes; UP000046393; Unplaced.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   CDD; cd08771; DLP_1; 1.
DR   CDD; cd01256; PH_dynamin; 1.
DR   Gene3D; 1.20.120.1240; Dynamin, middle domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 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   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   PANTHER; PTHR11566; DYNAMIN; 1.
DR   PANTHER; PTHR11566:SF212; DYNAMIN; 1.
DR   Pfam; PF01031; Dynamin_M; 1.
DR   Pfam; PF00350; Dynamin_N; 1.
DR   Pfam; PF02212; GED; 1.
DR   Pfam; PF00169; PH; 1.
DR   PRINTS; PR00195; DYNAMIN.
DR   SMART; SM00053; DYNc; 1.
DR   SMART; SM00302; GED; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS00410; G_DYNAMIN_1; 1.
DR   PROSITE; PS51718; G_DYNAMIN_2; 1.
DR   PROSITE; PS51388; GED; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   3: Inferred from homology;
KW   Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW   GTP-binding {ECO:0000256|RuleBase:RU003932};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW   Motor protein {ECO:0000256|ARBA:ARBA00023175};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU003932}.
FT   DOMAIN          30..296
FT                   /note="Dynamin-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51718"
FT   DOMAIN          520..625
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          655..747
FT                   /note="GED"
FT                   /evidence="ECO:0000259|PROSITE:PS51388"
FT   REGION          629..650
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          749..820
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        749..768
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        771..788
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   820 AA;  92540 MW;  DC02EDEE23EED6A5 CRC64;
     MAWANAGMQA LIPVVNRLQD AFAQLGTSLN FDLPQIAVVG GQSAGKSSVL ENFVGRDFLP
     RGSGIVTRRP LILQLIQDRA EYAEFLHKKG QKFVDFDLVR KEIEDETDRL TGQNKGISPV
     PINLRVFSPN VLNLTLIDLP GMTKVPVGDQ PPDIERQIVD MILTYISRET CLILAVTPAN
     SDLATSDALK LAREVDPQGL RTIGVITKLD LMDEGTDARD ILENRVFSLR RGYVGVVNRG
     QKDIMGKKDI RTALDAERRF FISHPAYRHM ADKLGTPYLQ KTLNQQLTNH IKDTLPALRD
     SLQKKLFTLE KDVAEYKNFS PNDPSRKTKV LMQMVQQFTV DIERSIEGSS AKTVSTNELS
     GGARINRLFH ERFPFEIVKM EIDEKEMRRE IHIAIRNIRG IRVGLFTPDM AFEAIVKKQI
     ERLKEPSLKC VDLVVNELAS VVRQCTECIA RYPRLRDEIE RIVTTNMREK EQIAKQQIAM
     IVDYELAYMN TNHEDFIGFS NYSAEAKASS SQTKKNLGNQ VIRKGWLSVH NISFVRGSKD
     CWFVLTSDSL SWYKDDEEKE KKYMLPLDGI MLRDLEAGFM SKQHKFALFY PDGKNIYKDY
     KQLELSASNL DEVDAWKASF LRAGVYPEKE KPAEEVENGR PEEDTSLDPQ LERQVETIRN
     LVDSYMRIVT KTIRDLVPKA IMYLIVNKVS NFLRDGELLA ALYQIGDTDS LMEESQLEAQ
     KREEMLRMYH ACKEALRIIG EVNMTTVSTE APPPVSTDWL SHGSHGSNGP SPVPRPAPQP
     PSGGQRPAPM PPRSGNRSAP SFANRPLPSA PGLPAPILPT
//