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Database: UniProt
Entry: A0A1I8Q4L8_STOCA
LinkDB: A0A1I8Q4L8_STOCA
Original site: A0A1I8Q4L8_STOCA 
ID   A0A1I8Q4L8_STOCA        Unreviewed;       840 AA.
AC   A0A1I8Q4L8;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=dynamin GTPase {ECO:0000256|ARBA:ARBA00011980};
DE            EC=3.6.5.5 {ECO:0000256|ARBA:ARBA00011980};
GN   Name=106092708 {ECO:0000313|EnsemblMetazoa:SCAU013872-PJ};
OS   Stomoxys calcitrans (Stable fly) (Conops calcitrans).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea;
OC   Muscidae; Stomoxys.
OX   NCBI_TaxID=35570 {ECO:0000313|EnsemblMetazoa:SCAU013872-PJ, ECO:0000313|Proteomes:UP000095300};
RN   [1] {ECO:0000313|EnsemblMetazoa:SCAU013872-PJ}
RP   IDENTIFICATION.
RC   STRAIN=USDA {ECO:0000313|EnsemblMetazoa:SCAU013872-PJ};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) 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   RefSeq; XP_013115135.1; XM_013259681.1.
DR   AlphaFoldDB; A0A1I8Q4L8; -.
DR   EnsemblMetazoa; SCAU013872-RJ; SCAU013872-PJ; SCAU013872.
DR   VEuPathDB; VectorBase:SCAU013872; -.
DR   OrthoDB; 1052588at2759; -.
DR   Proteomes; UP000095300; Unassembled WGS sequence.
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          23..289
FT                   /note="Dynamin-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51718"
FT   DOMAIN          513..622
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          657..748
FT                   /note="GED"
FT                   /evidence="ECO:0000259|PROSITE:PS51388"
FT   REGION          624..654
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          752..840
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        628..645
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        768..840
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   840 AA;  94067 MW;  F658A64F0EBFFDCC CRC64;
     MDSLIPIVNK LQDAFTQLGV HMQLDLPQIA VVGGQSAGKS SVLENFVGKD FLPRGSGIVT
     RRPLILQLIN GITEYGEFLH CKGKKFTSFD EVRKEIEDET DRVTGSNKGI SNIPINLRVH
     SPHVLNLTLI DLPGLTKVAI GDQPADIEQQ IRNMILQFIR KETCLILAVT PANTDLANSD
     ALKLAKEVDP QGIRTIGVIT KLDLMDEGTD ARDILENKLL PLRRGYIGVV NRSQKDIDGR
     KDIHMALAAE RKFFLSHPSY RHIADRLGTP YLQRVLNQQL TNHIRDTLPG LRDKLQKQML
     ALEKDVQEFK HFQPGDTSIK TKAMLQMIQQ LQSDFERTIE GSGSALVNTN ELSGGAKINR
     IFHERLRFEI VKMACDEKEL RREISFAIRN IHGIRVGLFT PDMAFEAIVK RQIAQLKEPV
     IKCVDLVVQE LSAVVRLCTD KMSRYPRLRE ETERIITTHI REREQLCKEQ ILLLIDFELA
     YMNTNHEDFI GFANAQNKSE NANKTGTRQL GNQVIRKGHM VIQNLGIMKG GGSRPYWFVL
     TSESISWYKD EDEKEKKYML PLDGLKLRDI EQGFMSMSRR VTFALFSPDG RNLYKDYKQL
     ELSCETVEDV ESWKASFLRA GVYPEKQETQ ENGDEEGREE KQASVETSTD PQLERQVETI
     RNLVDSYMKI VTKTTRDMVP KSIMMLIINN TKDFINGELL AHLYASGDQS QMMEESAEAA
     SKREEMLRMY HACKDALRII GDVSMATVSA PLPPPVKNDW LPSGLDNPRL SPPSPGGPRK
     PTPVAQPAAG GRGPPPPPAT GRPAPAIPNR PGGGAPPLPG GRPGGALPPP LLPSPFDEPL
//
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