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Database: UniProt
Entry: A0A151ILI7_9HYME
LinkDB: A0A151ILI7_9HYME
Original site: A0A151ILI7_9HYME 
ID   A0A151ILI7_9HYME        Unreviewed;       829 AA.
AC   A0A151ILI7;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=dynamin GTPase {ECO:0000256|ARBA:ARBA00011980};
DE            EC=3.6.5.5 {ECO:0000256|ARBA:ARBA00011980};
GN   ORFNames=ALC62_03584 {ECO:0000313|EMBL:KYN05491.1};
OS   Cyphomyrmex costatus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Cyphomyrmex.
OX   NCBI_TaxID=456900 {ECO:0000313|EMBL:KYN05491.1, ECO:0000313|Proteomes:UP000078542};
RN   [1] {ECO:0000313|EMBL:KYN05491.1, ECO:0000313|Proteomes:UP000078542}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MS0001 {ECO:0000313|EMBL:KYN05491.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KYN05491.1};
RA   Nygaard S., Hu H., Boomsma J., Zhang G.;
RT   "Cyphomyrmex costatus WGS genome.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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; KQ977133; KYN05491.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A151ILI7; -.
DR   STRING; 456900.A0A151ILI7; -.
DR   Proteomes; UP000078542; 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; 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   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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078542}.
FT   DOMAIN          29..295
FT                   /note="Dynamin-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51718"
FT   DOMAIN          519..625
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          655..746
FT                   /note="GED"
FT                   /evidence="ECO:0000259|PROSITE:PS51388"
FT   REGION          627..650
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          749..829
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        634..650
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        768..829
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   829 AA;  93306 MW;  004AFEC6322B4581 CRC64;
     MAGNTGMEQL IPIVNKLQDA FTQLGVHMQL DLPQIAVVGG QSAGKSSVLE NFVGKDFLPR
     GSGIVTRRPL ILQLINCLTE YAEFLHCKGK KFVDFDEVRK EIEAETDRVT GSNKGISNIP
     INLRVYSPNV LNLTLIDLPG LTKVPIGDQP ADIEAQIKAM IFQFIKRENC LILAVTPANT
     DLANSDALKL AKEVDAQGVR TIGVITKLDL MDDGTDARDI LENKLLPLRR GYIGVVNRSQ
     KDIEGRKDIK NALAAERKFF LSHPSYRHLA DRLGTPYLQR VLNQQLTNHI RDTLPALRDR
     LQKQQLTLEK DVEQYKHFRP DDPAIKTKAM LQMIQQLQSD FERTIEGSGS AQINTMELSG
     GAKINRLFHE RFPFEIVKME FDEKELRKEI AFAIRNIHGI RVGLFTPDMA FEAIVKKQIN
     RLKEPSLKCV DLVVQELSNV VRICTDRMSR YPRLREETER IITTYIRQRE QMCKEQLILL
     VDCELAYMNT NHEDFIGFAN AQQSSENAVK SGRHTLGNQV IRKGYMCIHN LGIMKGGSRD
     YWFVLTSESI SWFKDEEERE KKYMLPLDGL KLRDLEQGFM SRRHLFALFN PEGRNVYKDY
     KQLELSCETQ DDVDSWKASF LRAGVYPEKS TEQANGEEGG SEGQSSMDPQ LERQVETIRN
     LVDSYMKIVT KTTRDLVPKT IMHLIINNAK DFINGELLAH LYASGDQASM MEESPEEAQK
     REEMLRMYHA CKEALRIIGD VSMATVSTPV PPPVKNDWLI SGDNPRLSPP SPGGPRRGVT
     QPPPISSSRA PPPVPGSGRP APAIPNRPGP GGPPPTRANP GLPPPMIPS
//
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