ID V8NJ70_OPHHA Unreviewed; 865 AA.
AC V8NJ70;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=dynamin GTPase {ECO:0000256|ARBA:ARBA00011980};
DE EC=3.6.5.5 {ECO:0000256|ARBA:ARBA00011980};
GN Name=Dnm1 {ECO:0000313|EMBL:ETE61577.1};
GN ORFNames=L345_12670 {ECO:0000313|EMBL:ETE61577.1};
OS Ophiophagus hannah (King cobra) (Naja hannah).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus.
OX NCBI_TaxID=8665 {ECO:0000313|EMBL:ETE61577.1, ECO:0000313|Proteomes:UP000018936};
RN [1] {ECO:0000313|EMBL:ETE61577.1, ECO:0000313|Proteomes:UP000018936}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Blood {ECO:0000313|EMBL:ETE61577.1};
RX PubMed=24297900; DOI=10.1073/pnas.1314702110;
RA Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J.,
RA McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J.,
RA Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A.,
RA de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C.,
RA Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M.,
RA Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., Dirks R.P.,
RA Spaink H.P., Duboule D., McGlinn E., Kini R.M., Richardson M.K.;
RT "The king cobra genome reveals dynamic gene evolution and adaptation in the
RT snake venom system.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013).
CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC superfamily. Dynamin/Fzo/YdjA family. {ECO:0000256|RuleBase:RU003932}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETE61577.1}.
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DR EMBL; AZIM01003798; ETE61577.1; -; Genomic_DNA.
DR AlphaFoldDB; V8NJ70; -.
DR Proteomes; UP000018936; 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 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; IPR027417; P-loop_NTPase.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR11566; DYNAMIN; 1.
DR PANTHER; PTHR11566:SF23; DYNAMIN-2; 1.
DR Pfam; PF01031; Dynamin_M; 2.
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; 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:UP000018936}.
FT DOMAIN 28..294
FT /note="Dynamin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51718"
FT DOMAIN 548..654
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 750..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 807..865
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 778..792
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..842
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 865 AA; 97751 MW; 65F874371F909D98 CRC64;
MGNRGMEELI PLVNKLQDAF SSIGQSCHLD LPQIAVVGGQ SAGKSSVLEN FVGRDFLPRG
SGIVTRRPLI LQLIFSKTEY AEFLHCKSKK FTDFDEVRQE IEAETDRVTG TNKGISPIPI
NLRVYSPHVL NLTLIDLPGI TKVPVGDQPQ DIEYQIKDMI LQFISRESSL ILAVTPANMD
LANSDALKLA KEVDPQGLRT IGVITKLDLM DEGTDARDIL ENKLLPLRRG YIGVVNRSQK
DIDGKKDIRA ALAAERKFFL SHPAYRHMAD RMGTPHLQKV LNQQLTNHIR DTLPSLRSKL
QSQLLSLEKE VEEYKNFRPD DPTRKTKALL QMVQQFAVDF EKRIEGSGDQ VDTLELSGGA
RINRIFHERF PFELVKMEFD EKDLRREISY AIKNIHDLAF EAIVKKQVVK LKEPCLKCVD
LVIQELINTV RQTGLFTPDM AFEAIVKKQI IKLKEPSLKC VDLVVSELAM VIKKCSEKLG
SYPRLREETE RIVTTYIRER EGKTKDQILL LIDIELSYIN TNHEDFIGFA NAQQRSTQAN
KKRAIPNQVI RRGWLTINNI SIMKGGSKEY WFILTAESLS WYKDEEEKEK KYMLPLDNLK
IRDVEKGFMS NKHVFAIFNT EQRNVYKDLR QIELACDSQE DVDSWKASFL RAGVYPEKDQ
VENEDGAQEN TFSMDPQLER QVETIRNLVD SYTKDFIHSE LLAYLYSSAD QNSLMEESAD
QAQRRDDMLR MYHALKEALN IIGDITTSTV STPVPPPVDD TWLQAGSGGH SPTSQRRPPS
TVLPPPMPGP PLIPVPAAGS SSFVAPPIPS RPVPQSAFIT NNEPFSTPPQ IPSRPARIPP
GIPPAEDLLQ HRTGLPLSDQ LSPPC
//
