ID G8BVU5_TETPH Unreviewed; 862 AA.
AC G8BVU5;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Dynamin-type G domain-containing protein {ECO:0008006|Google:ProtNLM};
GN Name=TPHA0G01870 {ECO:0000313|EMBL:CCE64023.1};
GN OrderedLocusNames=TPHA_0G01870 {ECO:0000313|EMBL:CCE64023.1};
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:CCE64023.1, ECO:0000313|Proteomes:UP000005666};
RN [1] {ECO:0000313|EMBL:CCE64023.1, 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; CCE64023.1; -; Genomic_DNA.
DR RefSeq; XP_003686457.1; XM_003686409.1.
DR AlphaFoldDB; G8BVU5; -.
DR STRING; 1071381.G8BVU5; -.
DR GeneID; 11535928; -.
DR KEGG; tpf:TPHA_0G01870; -.
DR eggNOG; KOG0446; Eukaryota.
DR HOGENOM; CLU_008640_0_1_1; -.
DR OMA; PLKMGYV; -.
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; 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; IPR030381; G_DYNAMIN_dom.
DR InterPro; IPR020850; GED_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11566; DYNAMIN; 1.
DR PANTHER; PTHR11566:SF237; INTERFERON-INDUCED GTP-BINDING PROTEIN MX; 1.
DR Pfam; PF00350; Dynamin_N; 1.
DR PRINTS; PR00195; DYNAMIN.
DR SMART; SM00053; DYNc; 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 202..483
FT /note="Dynamin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51718"
FT DOMAIN 758..850
FT /note="GED"
FT /evidence="ECO:0000259|PROSITE:PS51388"
FT REGION 124..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 862 AA; 97798 MW; B4243AFA52DD70AB CRC64;
MIPFLNRTTQ KNSSLILNYS KCYRKLLSSQ SILTNQLSSR NLITYGKRQS VLHNRSVYLV
NSEVINVKRF VSTFVPKLIT RVIKVPAYIG GLFAATGSYI AYKVEGLKEN EYLSNLRDFF
NDMLSNPDGS QNGNNNNNDN NTGSSVAMST GIIASTQNDE DDSEDDDLLD EVDNTNDVML
NLTKQMIEIR SILNRIDTNS SHLTLPSIVV IGSQSSGKSS VLESIVGKQF LPKGSNMVTR
RPIELTLVNT PNSKETTADF PSLRIYNLTD FQEVERLLVD ANLSVPIRDA ISEEPIQLTI
KSPNVPDLSL VDLPGYIQIE AADQPIELKS KILKVCDNYL QAPNIILAIS SADVDLANSS
ALMASKKVDP TGSRTIGVIT KLDLVDTETA KAILNNKKYP LKMGYVGVIT KSMNNKKSSL
FEYSKSGKDK NLLSQSKQNA TKQFERSYFA EHKDAFKNCQ VSTKKLREKL IKILEISMSD
ALEPTSKLIQ QSLDDTAYHF KVEFNDRQLT AKSYLLNNVD IFKLAIKQFQ ENFNRAEPTS
ILKADLDQNV LDFLATRYWK DENLSELSSN DISENEMLYW HKKLDLASSS LTKIGIGRKS
TTLITNAILR ELNNILDNSQ LKNHDLIKDL VTDTAATVLN SKYYTTTDQV ENCIKPFKYE
IDIEERDWII SREHAVNLLK EELKQCNEKY QTIRNAIGSR KLQHVISYLQ KHKPSDNKET
LGMSKLLLER GAEAMFLEKR SKVLNFRLKL LRTKCNSTSE KDKCPEIFLD AVSDKLTSTA
VLFLNVELLS DFFYNFPIEL DRKLNLLTNE QIELFAKEDP KISRHIELQK RKELLELALS
KIDSLLVFRK SYKGMAKRNY RD
//
