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Database: UniProt
Entry: A0A158QLN6_HAEPC
LinkDB: A0A158QLN6_HAEPC
Original site: A0A158QLN6_HAEPC 
ID   A0A158QLN6_HAEPC        Unreviewed;       849 AA.
AC   A0A158QLN6;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=dynamin GTPase {ECO:0000256|ARBA:ARBA00011980};
DE            EC=3.6.5.5 {ECO:0000256|ARBA:ARBA00011980};
GN   ORFNames=HPLM_LOCUS6813 {ECO:0000313|EMBL:VDO30106.1};
OS   Haemonchus placei (Barber's pole worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Trichostrongylidae; Haemonchus.
OX   NCBI_TaxID=6290 {ECO:0000313|Proteomes:UP000038042, ECO:0000313|WBParaSite:HPLM_0000682101-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:HPLM_0000682101-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (APR-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDO30106.1, ECO:0000313|Proteomes:UP000268014}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHpl1 {ECO:0000313|EMBL:VDO30106.1,
RC   ECO:0000313|Proteomes:UP000268014};
RG   Pathogen Informatics;
RL   Submitted (NOV-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; UZAF01016552; VDO30106.1; -; Genomic_DNA.
DR   STRING; 6290.A0A158QLN6; -.
DR   WBParaSite; HPLM_0000682101-mRNA-1; HPLM_0000682101-mRNA-1; HPLM_0000682101.
DR   OMA; FIGFANM; -.
DR   Proteomes; UP000038042; Unplaced.
DR   Proteomes; UP000268014; 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:UP000268014}.
FT   DOMAIN          30..316
FT                   /note="Dynamin-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51718"
FT   DOMAIN          540..645
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          686..777
FT                   /note="GED"
FT                   /evidence="ECO:0000259|PROSITE:PS51388"
FT   REGION          776..849
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        779..849
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   849 AA;  95932 MW;  B77BC0D2F1D193DB CRC64;
     MAWVNQGMQA LIPVINRVQD AFSQLGTSVN FELPQIAVVG GQSAGKSSVL ENFVGRDFLP
     RGSGIVTRRP LILQLIQDRN EYAEFLHKKG TYFSDFDAVR KEIEDETDRV TGLNKGISPH
     PINLRVFSPN VLNLTLIDLP GLTKVPVGDQ PPDIEHQIRE MILTFISRET CLILAVTPAN
     SDLATSDALK LAKVLCLAEC YEWLLLHNKS FFQEVDPQGL RTIGVLTKLD LMDEGTDARD
     ILENRLFPLR RGYVGVVNRG QKDIVGKKDI RAALDAERKF FLSHPAYRHM ADRLGTQFLQ
     HTLNQQLTNH IRDTLPTLRD SLQKKLFALE KDVAEYKNFQ PNDPGRKTKA LLQMVQQFTV
     DIERSIEGSS AKLVSTNELS GGARINRLFH ERFPFEIVKM EIDEKEMRKE IQFAIRNIHG
     IRVGLFTPDM AFEAIAKKQI ARLKEPSLKC VDLVVNELAN VIRQCAECLS RYPRLRDEIE
     RIVVTRVREK EQYAKNQISL IVDYELAYMN TNHEDFIGFS NAEAKASQGQ ASSKKNLGVQ
     VIRKGWLSIN NISFIKGSKD CWFVLMSDSL SWFKDDEEKE KKYMLPLDGI KLRDIESGFM
     SRQHKFALFY PDGKNIYKDY KQLELGCNNL DEVDAWKASF LRAGVYPEKQ KAVAEDEARG
     VLIRNCLFNQ VEVEETSMDP QLERQVETIR NLVDSYMRII TKTIKDLVPK AIMHLIVSQV
     TQFMHDELLA HIYQCGDTDS LMEESQIEAQ KREEMLRMYH ACKEALRIIS EVNMSTLGDT
     PPPLPPSDYR PMPSGPSPVP RPAPAPPGGR HAPMPPRPGP GGPGGPPPHR GPPGPPPGQG
     AYPPPLIPT
//
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