ID G3AR76_SPAPN Unreviewed; 850 AA.
AC G3AR76;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Dynamin-related GTPase {ECO:0008006|Google:ProtNLM};
GN ORFNames=SPAPADRAFT_139974 {ECO:0000313|EMBL:EGW31251.1};
OS Spathaspora passalidarum (strain NRRL Y-27907 / 11-Y1).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Spathaspora.
OX NCBI_TaxID=619300 {ECO:0000313|Proteomes:UP000000709};
RN [1] {ECO:0000313|EMBL:EGW31251.1, ECO:0000313|Proteomes:UP000000709}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-27907 / 11-Y1 {ECO:0000313|Proteomes:UP000000709};
RX PubMed=21788494; DOI=10.1073/pnas.1103039108;
RA Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A., LaButti K.M.,
RA Sun H., Clum A., Pangilinan J.L., Lindquist E.A., Lucas S., Lapidus A.,
RA Jin M., Gunawan C., Balan V., Dale B.E., Jeffries T.W., Zinkel R.,
RA Barry K.W., Grigoriev I.V., Gasch A.P.;
RT "Comparative genomics of xylose-fermenting fungi for enhanced biofuel
RT production.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(2011).
CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC superfamily. Dynamin/Fzo/YdjA family. {ECO:0000256|RuleBase:RU003932}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GL996503; EGW31251.1; -; Genomic_DNA.
DR RefSeq; XP_007376029.1; XM_007375967.1.
DR AlphaFoldDB; G3AR76; -.
DR STRING; 619300.G3AR76; -.
DR GeneID; 18870257; -.
DR KEGG; spaa:SPAPADRAFT_139974; -.
DR eggNOG; KOG0446; Eukaryota.
DR HOGENOM; CLU_008964_5_0_1; -.
DR InParanoid; G3AR76; -.
DR OMA; KICHNCG; -.
DR OrthoDB; 1052588at2759; -.
DR Proteomes; UP000000709; 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; 2.
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:UP000000709}.
FT DOMAIN 25..361
FT /note="Dynamin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51718"
FT DOMAIN 763..850
FT /note="GED"
FT /evidence="ECO:0000259|PROSITE:PS51388"
FT REGION 79..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..93
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..645
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 850 AA; 95935 MW; C4C75CE4539919B4 CRC64;
MSSLQDLIPV VNKLQDIITT TQLADIDLPI LAVVGSQSCG KSSVLENIVG KDFLPRGTGI
VTRRPLVLQL INISDEENDS NTTDFYSTSA PVSDEDGSHH HRGYDRQHPQ IPNGHFSYST
DDVGSVNLED HIRNMSNGKT TRSSREWGEF LHVPNKRFYD FHDIRREIEH ETMRIAGQNK
GISRLPINLK IYSPNVLNLT LVDLPGLTKI PIGDQPTDIE KQTRNLILEY ISNPNCIILA
VSPANVDLVN SESLKLARQV DPMGKRTVGI LTKLDLMDQG TNALDILKGN VYPLKLGFIG
IVNRSQQDIS ENKPLDESLN AEQRFFLNHP AYKAMASKCG TKYLSVTLNK ILMAHIRERL
PDIKAKLNTL RGQTEQELAS YGDEFSEGEG EARGAKVLTL MTKFAQAFIS SIEGTASSAA
FNDVSTKELC GGARIYYIYN EIFGSQLASI NPTHNLSILD IRTAIRNSTG PRPSLFVPEL
AFDLLVKPQI KLLQDPSRHC VELVYEELMK IVHNVCSSAI IGPELTRYPK LQSKLIEVVS
DLLRERLGPT IKYVESLIEI HRAYINTNHP SFLGAAKAMS IVVSERQKQK QLESDSKLRL
ASERILSKNI KQSGSDDEEE EESDEPTDIN QEIKSVDDVI PSKHKHKKSV KEFTPPVNSN
NPDSYLNYFL GKDPIVHQQH LQQQAQLHPV PFKYPVHQEQ VLQFNTNYIP SHNSEFNSNQ
LSPDSHLSDQ FNSKMVMSDS IDDGSFTSDE TINELTEREQ LECELIRRLI ISYFGIVREM
IQDQVPKSIM CLLVNYIKQH IQNRLVVKLY NDNLFDELLK EDEAIQAERE KCLELLKTYK
EASRIISDVV
//