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Database: UniProt
Entry: G3AR76_SPAPN
LinkDB: G3AR76_SPAPN
Original site: G3AR76_SPAPN 
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}.
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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
//
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