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Database: UniProt
Entry: A0A158QA76_ENTVE
LinkDB: A0A158QA76_ENTVE
Original site: A0A158QA76_ENTVE 
ID   A0A158QA76_ENTVE        Unreviewed;       803 AA.
AC   A0A158QA76;
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=EVEC_LOCUS4028 {ECO:0000313|EMBL:VDD89277.1};
OS   Enterobius vermicularis (Human pinworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Oxyuridomorpha; Oxyuroidea; Oxyuridae; Enterobius.
OX   NCBI_TaxID=51028 {ECO:0000313|Proteomes:UP000038041, ECO:0000313|WBParaSite:EVEC_0000432001-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:EVEC_0000432001-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (APR-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDD89277.1, ECO:0000313|Proteomes:UP000274131}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (OCT-2018) 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; UXUI01007743; VDD89277.1; -; Genomic_DNA.
DR   STRING; 51028.A0A158QA76; -.
DR   WBParaSite; EVEC_0000432001-mRNA-1; EVEC_0000432001-mRNA-1; EVEC_0000432001.
DR   Proteomes; UP000038041; Unplaced.
DR   Proteomes; UP000274131; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000274131}.
FT   DOMAIN          30..296
FT                   /note="Dynamin-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51718"
FT   DOMAIN          511..616
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          644..736
FT                   /note="GED"
FT                   /evidence="ECO:0000259|PROSITE:PS51388"
FT   REGION          618..640
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          742..803
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        618..639
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        755..772
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        773..787
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   803 AA;  90818 MW;  B4B62DB26902F4C9 CRC64;
     MAWANTGMQA LIPVVNRLQD AFAQLGTSLN FDLPQIAVVG GQSAGKSSVL ENFVGRDFLP
     RGSGIVTRRP LILQLIQDRA EYAEFLHKKG QKFVDFDLVR KEIEDETDRL TGLNKGISPV
     PINLRVFSPN VLNLTLIDLP GMTKVPVGDQ PPDIERQITD MILTYISRET CLILAVTPAN
     SDLATSDALK LAREVDPQGL RTIGVITKLD LMDEGTDARD ILENRVFSLR RGYVGVVNRG
     QKDIMGKKDI RAALDAERKF FISHPAYRHM ADRLGTPYLQ KTLNQQLTNH IKDTLPALRD
     SLQKKLFALE KDVAEYKNFS PNDPSRKTKQ FTVDIERSIE GSSAKTVSTN ELSGGARINR
     LFHERFPFEI VKMEIDEKEM RREIHIAIRN IRGIRVGLFT PDMAFEAIVK KQIERLKEPS
     LKCVDLVVNE LANVVRQCTE CVARYPRLRD EIERIVTTNM REKEQIAKQQ ISMIVDYELA
     YMNTNHEDFI GFSNAEAKAS SAQTKKNLGN QVIRKGWLSV HNISFVRGSK DCWFVLTSDN
     LSWYKDDEEK EKKYMLPLDG IMLRDLEAGF MSRQHKFALF YPDGKNIYKD YKQLELSASN
     LDEVDAWKAS FLRAGVYPEK EKPTEENGRT EEETSLDPQL ERQVETIRNL VDSYMRIVTK
     TIRDLVPKAI MFLIVNKVSS FLRDGELLAS LYQIGDTESL MEESQLEAQK REEMLRMYHA
     CKEALRIIGE VNMTTVATEA PPAVSTDWMR SNGPSPVPRP APQPPTGQRP APMPPRSANQ
     SAPSFANRPL PTAPGLPAPL LPT
//
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