ID G8BW97_TETPH Unreviewed; 712 AA.
AC G8BW97;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE RecName: Full=Dynamin-type G domain-containing protein {ECO:0008006|Google:ProtNLM};
GN Name=TPHA0G03350 {ECO:0000313|EMBL:CCE64175.1};
GN OrderedLocusNames=TPHA_0G03350 {ECO:0000313|EMBL:CCE64175.1};
OS Tetrapisispora phaffii (strain ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL
OS Y-8282 / UCD 70-5) (Yeast) (Fabospora phaffii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX NCBI_TaxID=1071381 {ECO:0000313|EMBL:CCE64175.1, ECO:0000313|Proteomes:UP000005666};
RN [1] {ECO:0000313|EMBL:CCE64175.1, ECO:0000313|Proteomes:UP000005666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL Y-8282 / UCD 70-5
RC {ECO:0000313|Proteomes:UP000005666};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(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; HE612862; CCE64175.1; -; Genomic_DNA.
DR RefSeq; XP_003686609.1; XM_003686561.1.
DR AlphaFoldDB; G8BW97; -.
DR STRING; 1071381.G8BW97; -.
DR GeneID; 11535813; -.
DR KEGG; tpf:TPHA_0G03350; -.
DR eggNOG; KOG0446; Eukaryota.
DR HOGENOM; CLU_008964_5_0_1; -.
DR OMA; IQRRKEC; -.
DR OrthoDB; 1052588at2759; -.
DR Proteomes; UP000005666; Chromosome 7.
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:SF220; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 1; 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:UP000005666}.
FT DOMAIN 26..341
FT /note="Dynamin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51718"
FT DOMAIN 626..712
FT /note="GED"
FT /evidence="ECO:0000259|PROSITE:PS51388"
SQ SEQUENCE 712 AA; 79271 MW; 541FA09230E9D9BC CRC64;
MDEYLISTIN KLQDALAPLG GGSQSPIDLP QITVVGSQSS GKSSVLENIV GRDFLPRGTG
IVTRRPLVLQ LINRRAANDD SSSNDNVKST TNELLDLDLD DKKAKAYEKN NNSNAVKGQA
EDNQDEWGEF LHLPDRKFFN FEEIRQEIVR ETDKVTGGNL GISSVPINLR IYSPHVLTLT
LVDLPGLTKV PVGDQPPDIE RQIKDMLLKY ISKPNAIILS VNAANTDLAN SDGLKLAREV
DPEGTRTIGV LTKVDLMDQG TDVIDILAGR VIPLRYGYIP VINRGQKDIE HKKTIRAALD
DERKFFEGHS SYSSKAQYCG TPYLAKKLNS ILLHHIRQTL PEIKAKIEAT LKKYQSELFN
LGPETMDSSN SIVLSMITDF SNEYAGILDG EAKEMSSNEL SGGARVSFVF HEVFKNGIDS
LDPFDQIKDS DIRTIMYNSS GSAPSLFVGT EAFEVLVKQQ IKRFEEPSLK LISLVFDELV
RMLKQIIKQP KYSRYPALRE AISNQFIEYL KEAIIPTNEF VVDIIKAEET YINTAHPDLL
KGSQAMAMVD EKLHPRQVAV DPKTGKPLPN SAAVPATPAV PSPEEKSGFF GGFFSSKNKK
KLASLESPPP VLKATGQMTD RETMETEVIK LLISSYFNIV KRTVADVIPK ALMLKLIVKS
RTDIQKVLLE KLYNERNIEE LTKENDGTIQ RRLECKKMVD ILRHASEIVS SV
//