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
//