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Database: UniProt
Entry: C4R5G4_KOMPG
LinkDB: C4R5G4_KOMPG
Original site: C4R5G4_KOMPG 
ID   C4R5G4_KOMPG            Unreviewed;       791 AA.
AC   C4R5G4;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   28-JUN-2023, entry version 86.
DE   SubName: Full=Dynamin-related GTPase {ECO:0000313|EMBL:CAY70800.1};
GN   OrderedLocusNames=PAS_chr3_0751 {ECO:0000313|EMBL:CAY70800.1};
OS   Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Komagataella.
OX   NCBI_TaxID=644223 {ECO:0000313|EMBL:CAY70800.1, ECO:0000313|Proteomes:UP000000314};
RN   [1] {ECO:0000313|EMBL:CAY70800.1, ECO:0000313|Proteomes:UP000000314}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GS115 / ATCC 20864 {ECO:0000313|Proteomes:UP000000314};
RX   PubMed=19465926; DOI=10.1038/nbt.1544;
RA   De Schutter K., Lin Y.C., Tiels P., Van Hecke A., Glinka S.,
RA   Weber-Lehmann J., Rouze P., Van de Peer Y., Callewaert N.;
RT   "Genome sequence of the recombinant protein production host Pichia
RT   pastoris.";
RL   Nat. Biotechnol. 27:561-566(2009).
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; FN392321; CAY70800.1; -; Genomic_DNA.
DR   RefSeq; XP_002492979.1; XM_002492934.1.
DR   AlphaFoldDB; C4R5G4; -.
DR   SMR; C4R5G4; -.
DR   STRING; 644223.C4R5G4; -.
DR   EnsemblFungi; CAY70800; CAY70800; PAS_chr3_0751.
DR   GeneID; 8200444; -.
DR   KEGG; ppa:PAS_chr3_0751; -.
DR   eggNOG; KOG0446; Eukaryota.
DR   HOGENOM; CLU_008964_5_0_1; -.
DR   InParanoid; C4R5G4; -.
DR   OMA; KICHNCG; -.
DR   OrthoDB; 1052588at2759; -.
DR   Proteomes; UP000000314; Chromosome 3.
DR   GO; GO:0032153; C:cell division site; IEA:EnsemblFungi.
DR   GO; GO:0005739; C:mitochondrion; IEA:EnsemblFungi.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0034643; P:establishment of mitochondrion localization, microtubule-mediated; IEA:EnsemblFungi.
DR   GO; GO:0090149; P:mitochondrial membrane fission; IEA:EnsemblFungi.
DR   GO; GO:0000001; P:mitochondrion inheritance; IEA:EnsemblFungi.
DR   GO; GO:0007031; P:peroxisome organization; IEA:EnsemblFungi.
DR   GO; GO:0140572; P:vacuole fission; IEA:EnsemblFungi.
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:UP000000314}.
FT   DOMAIN          25..339
FT                   /note="Dynamin-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51718"
FT   DOMAIN          704..791
FT                   /note="GED"
FT                   /evidence="ECO:0000259|PROSITE:PS51388"
FT   REGION          79..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          551..626
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        99..113
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        551..575
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        576..602
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        603..623
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   791 AA;  88512 MW;  65241FB5D11D48FA CRC64;
     MSALKDLIPV VNKLQDIVTT TNLTELDLPL LTIIGSQSAG KSSVLENIVG KDFLPRGTGI
     VTRRPLILQL INIQPDDPLV YQNSSSSGPG YPESSDVAEE PTLEDHLRKN ADPSGADDQS
     PVAEWGQFLH LPGKRFYNFQ EIRREIEAET ARIAGKNKGI SRVPINLKIY SPNVLNLTMV
     DLPGLTKIPI GDQPTDIERQ IKNLILEYIA RPNAIILAVS PANVDLVNSE ALKLARQVDP
     QGKRTIGVLS KVDLMDHGTN ALDILTGKVY PLKLGFIGVV NRSQQDISVN KALFDSLRAE
     EEFFQSHAAY RNIANRCGTK YLARVLNQTL MNHIRERLPD IKAKLNTLMG QTEQELASYG
     DMGSVSESNK GGLILQLMTK FATNFVNSIE GNSSSVSTKE LCGGARIYSI YNDVFGSSLL
     SINPTASLSV SDIRTAIRNS TGPRPSLFVP ELAFDLLVKP QIKLLEGPSH RCVELVYEEL
     MKICHNCGSP ELGRYPKLQA KLIEVISDLL RERLGPTTQY VESLIDIHRA YINTNHPNFV
     GAAAAMTSVV EERKKQKEES MRIKTREEKK KSTETGSASS PDSPKELLLE NGSTNSSVSQ
     LIEKHRKSSD SVHGDDSRHA QQQNGDNKES FLNFFFGKDS QQENQQQQLH QNKPATRPFQ
     FAEDSETLHF SNEPEAQTAI QRMDALNLHK DTEAHLSERE QLECELIRRL IDSYFDIVRE
     MIQDQVPKAV MCLLVNYTKE CVQNRLVSKL YKESMFDELL FEDENLAQER EKCQKLLNTY
     KEASEIINEV I
//
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