ID A0A452IV10_9SAUR Unreviewed; 861 AA.
AC A0A452IV10;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=dynamin GTPase {ECO:0000256|ARBA:ARBA00011980};
DE EC=3.6.5.5 {ECO:0000256|ARBA:ARBA00011980};
OS Gopherus agassizii (Agassiz's desert tortoise).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Testudinidae; Gopherus.
OX NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000031876.1, ECO:0000313|Proteomes:UP000291020};
RN [1] {ECO:0000313|Proteomes:UP000291020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28562605;
RA Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT "The Agassiz's desert tortoise genome provides a resource for the
RT conservation of a threatened species.";
RL PLoS ONE 12:e0177708-e0177708(2017).
RN [2] {ECO:0000313|Ensembl:ENSGAGP00000031876.1}
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; A0A452IV10; -.
DR Ensembl; ENSGAGT00000036153.1; ENSGAGP00000031876.1; ENSGAGG00000022886.1.
DR Proteomes; UP000291020; 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:SF32; DYNAMIN-1; 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:UP000291020}.
FT DOMAIN 28..294
FT /note="Dynamin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51718"
FT DOMAIN 515..621
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 655..746
FT /note="GED"
FT /evidence="ECO:0000259|PROSITE:PS51388"
FT REGION 764..861
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 778..861
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 861 AA; 96923 MW; A09DE8326995409E CRC64;
MGNRGMEDLI PLVNKLQDAF ASIGQNADLD LPQIAVVGGQ SAGKSSVLEN FVGRDFLPRG
SGIVTRRPLV LQLVNSTTEF GEFLHCKGKK FTDFEEIRLE IEAETDRVTG SNKGISSVPI
NLRVYSPHVL SLTLVDLPGM TKVPVGDQPL DIEFQIREMI MQFVTKENCL ILAVSPANSD
LANSDALKIA KEVDPQGQRT IGVITKLDLM DEGTDARDVL ENKLLPLRRG YIGVVNRSQK
DIDGKKDIQA ALAAERKFFL SHPSYRHMAE RMGTPYLQKV LNQQLTNHIR DTLPGLRNKL
QSQLLSIEKE VDEYKNFRPD DPARKTKALL QMVQQFAVDF EKRIEGSGDQ IDTYELSGGA
RINRIFHERF PFELVKMEFD EKELRREISY AIKNIHGIRT GLFTPDMAFE TIVKKQVKKI
KEPCLKCVDM VISELINTVR QCTKKLSQYP HLREEMDRIV TTHIREREGR TKDQVMLLID
IELAYMNTNH EDFIGFANAQ QRSSQMSKKK AAGNQVIRKG WLTINNIGIM KGGAKEYWFV
LTAENLSWYK DDEEKEKKYM LPVDNLKLRD IEKGFMSSKH IFALFNTEQR NVYKDYRQLE
LACETQEEVD SWKASFLRAG VYPERVGDKD KANETEENGS DSFMHSMDPQ LERQVETIRN
LVDSYMGIVN KTIRDLMPKT IMHLMINNTK DFIHSELLAN LYSCGDQNSL MEESVEQAQR
RDEMLRMYHA LKEALSIIGD INTSTISTPT PPPVDDSWLQ VQSIPSGRRS PTSSPTPQRR
APAVPPARPV SRGPAPGPPP AGGPTLGGAP PVPSRPGASP DPFGPPPQVP SRPNRAPPGV
PSRPGKASPS RPESPKPPFE M
//
