ID A0A0C7NB27_9SACH Unreviewed; 766 AA.
AC A0A0C7NB27;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=LALA0S06e02542g1_1 {ECO:0000313|EMBL:CEP62732.1};
GN ORFNames=LALA0_S06e02542g {ECO:0000313|EMBL:CEP62732.1};
OS Lachancea lanzarotensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=1245769 {ECO:0000313|EMBL:CEP62732.1, ECO:0000313|Proteomes:UP000054304};
RN [1] {ECO:0000313|EMBL:CEP62732.1, ECO:0000313|Proteomes:UP000054304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 12615 {ECO:0000313|EMBL:CEP62732.1,
RC ECO:0000313|Proteomes:UP000054304};
RA Neuveglise Cecile;
RL Submitted (DEC-2014) 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; LN736365; CEP62732.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C7NB27; -.
DR STRING; 1245769.A0A0C7NB27; -.
DR HOGENOM; CLU_008964_5_0_1; -.
DR OrthoDB; 1052588at2759; -.
DR Proteomes; UP000054304; Unassembled WGS sequence.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0006996; P:organelle organization; IEA:UniProt.
DR CDD; cd08771; DLP_1; 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 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 PANTHER; PTHR11566; DYNAMIN; 1.
DR PANTHER; PTHR11566:SF21; DYNAMIN-1-LIKE PROTEIN; 1.
DR Pfam; PF01031; Dynamin_M; 1.
DR Pfam; PF00350; Dynamin_N; 1.
DR Pfam; PF02212; GED; 1.
DR PRINTS; PR00195; DYNAMIN.
DR SMART; SM00053; DYNc; 1.
DR SMART; SM00302; GED; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00410; G_DYNAMIN_1; 1.
DR PROSITE; PS51718; G_DYNAMIN_2; 1.
DR PROSITE; PS51388; GED; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|RuleBase:RU003932};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU003932};
KW Reference proteome {ECO:0000313|Proteomes:UP000054304}.
FT DOMAIN 25..335
FT /note="Dynamin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51718"
FT DOMAIN 679..766
FT /note="GED"
FT /evidence="ECO:0000259|PROSITE:PS51388"
FT REGION 573..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..610
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 766 AA; 85740 MW; 22D462E755E33E19 CRC64;
MASLEDLIPT ANKLQDVMYD AGIDTLDLPV LAVIGSQSSG KSSILETLVG KDFLPRGTGI
VTRRPLVLQL NNVAPNSPLI KEHHGEFESS VTQANDNTSE LTLEDHLRKN QGFESVDRSE
WGEFLHLPGR RFYDFAEIRN EIQNETARIA GKNKGISRIP INLKVYSPRV LNLTLVDLPG
ITKVPIGEQP ADIERQIKNL ILEYVAKPNC IILAVSPANV DLVNSESLKL AREVDPHGRR
TIGVITKMDL MDGGTNALDI LSGKLYPLKL GFVGVVNRSQ QDIQSNISVE EALDNEEAFF
VRHPVYRTIS TRCGTRYLAK LLNHILLNHI RDKLPDIKAR LNTLIGQTEQ ELQTYGGTGA
ITKENRAGLV LQLMNKFAAR FVSSIEGTST DIGTKELCGG ARIYFIYNNI FGSSLKSISP
TENLSTRDIQ TAIRNSTGPR PSLFVPELAF DLLVKPQIQL LLEPSERCVE LVYEELMKIC
HNCGTPELAR YPKLQAKLIE VVSELLRERL GPTRSYVESL IEIHRAYINT NHPNFLSATE
VMAGIVDGRK GGKVQSAKKP DLEDARQSIA KDLVKKHNED SSPTLTSISD SEKNRSSEAF
SDDENDSSKQ SKDSFLNYFF GKDQQGSHQL NGSTEEYNLN SNKQRVTDLA ELDKLHLTDG
GQNIENLLPQ MSEREQLECE LISRLIVSYF GIVREMIQDQ IPKAVMCLLV NFSKEIIQNR
LVTKLYKESL FEDLLMEDQN LAQDRQKCVK LLETYKAASH IMNDIL
//