ID   A0A3B3S8J6_9TELE        Unreviewed;       847 AA.
AC   A0A3B3S8J6;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=dynamin GTPase {ECO:0000256|ARBA:ARBA00011980};
DE            EC=3.6.5.5 {ECO:0000256|ARBA:ARBA00011980};
OS   Paramormyrops kingsleyae.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC   Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX   NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000026525.1, ECO:0000313|Proteomes:UP000261540};
RN   [1] {ECO:0000313|Ensembl:ENSPKIP00000026525.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) 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   AlphaFoldDB; A0A3B3S8J6; -.
DR   STRING; 1676925.ENSPKIP00000026525; -.
DR   Ensembl; ENSPKIT00000007282.1; ENSPKIP00000026525.1; ENSPKIG00000008976.1.
DR   GeneTree; ENSGT00940000155764; -.
DR   OrthoDB; 1052588at2759; -.
DR   Proteomes; UP000261540; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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:SF54; DYNAMIN-3; 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   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, 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|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU003932}.
FT   DOMAIN          28..294
FT                   /note="Dynamin-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51718"
FT   DOMAIN          525..631
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          659..750
FT                   /note="GED"
FT                   /evidence="ECO:0000259|PROSITE:PS51388"
FT   REGION          747..847
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        747..778
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        788..808
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        823..839
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   847 AA;  94697 MW;  52BD9B71682C54D2 CRC64;
     MGNRGMEDLI PLVNRLQDAF SAIGQSCNLD LPQIAVVGGQ SAGKSSVLEN FVGRDFLPRG
     SGIVTRRPLV LQLISSNAEY AEFLHCKGKK FTDFDEVRLE IEAETDRLTG ANKGISPVPI
     NLRVCSPHVL NLTLIDLPGI TKVPVGDQPA DIEYQIRDMI MQFICRENCL ILAVTPANTD
     LANSDALKLA KDVDPQGLRT IGVMTKLDLM DEGTDARDVL ENKLLPLRRG YIGVVNRSQK
     DIEGKKDIKA ALAAERKFFL SHPAYRHIAD SMGTPHLQRA LNQQLTNHIR DTLPAFRSKL
     QTQLLALDKE AEEYRHFRPD DPSRKTKALL QMVQQFSVDF EKRIEGSGDQ VDTVELSGGA
     KINRIFHERF PFELVKMEFD EKDLRREISY AIKNIHGIRT GLFTPDLAFE AIVKKQIVKL
     KGPCLKCVDM VIQELVSTVR QCTVKLGSFP RLREETERIV TTHIRDRESR AKDQVLLLIE
     VQLSYINTNH EDFIGFANAQ QRSTTMSQKS SAGNQGAAPP PPSQIVIRKG WLTINNISII
     KGGAKEYWFV LTAESLSWFK DDEEKEKKYM LPLDNLKVRD VEKGFMSSKH IFAIFNIEQR
     NVYKDYRFLE LACDTQDDVD SWKASLLRAG VYPEKVSADG ENSGPSDSFS MDPQLERQVE
     TIRNLVDSYM AIVNKCIRDL MPKTIMHLMI INVKEFINAE LLAQLYSTGD QNALMDESPE
     QAQRRDEVLR THHALTEALA IIGDISTSTI STPLPPPVDS SWLQAGSGRR SPPLSPTASK
     RFPSGPRAPA RGPAPTAPPV PSRPGPPGPF NNSSDAFQPP QVPNRPNRAP PSIPRRHPPA
     VPSRPEH
//