ID A0A2G5V4C9_9PELO Unreviewed; 775 AA.
AC A0A2G5V4C9;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Dynamin-type G domain-containing protein {ECO:0000259|PROSITE:PS51718};
GN Name=Cni-fzo-1 {ECO:0000313|EMBL:PIC46645.1};
GN Synonyms=Cnig_chr_II.g6265 {ECO:0000313|EMBL:PIC46645.1};
GN ORFNames=B9Z55_006265 {ECO:0000313|EMBL:PIC46645.1};
OS Caenorhabditis nigoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1611254 {ECO:0000313|EMBL:PIC46645.1, ECO:0000313|Proteomes:UP000230233};
RN [1] {ECO:0000313|Proteomes:UP000230233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JU1422 {ECO:0000313|Proteomes:UP000230233};
RA Yin D., Schwarz E.M., Thomas C.G., Felde R.L., Korf I.F., Cutter A.D.,
RA Schartner C.M., Ralston E.J., Meyer B.J., Haag E.S.;
RT "Rapid genome shrinkage in a self-fertile nematode reveals novel sperm
RT competition proteins.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000256|ARBA:ARBA00001270};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion
CC outer membrane {ECO:0000256|ARBA:ARBA00004374}; Multi-pass membrane
CC protein {ECO:0000256|ARBA:ARBA00004374}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PIC46645.1}.
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DR EMBL; PDUG01000002; PIC46645.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5V4C9; -.
DR STRING; 1611254.A0A2G5V4C9; -.
DR Proteomes; UP000230233; Chromosome ii.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0008053; P:mitochondrial fusion; IEA:InterPro.
DR CDD; cd09912; DLP_2; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR045063; Dynamin_N.
DR InterPro; IPR006884; Fzo/mitofusin_HR2.
DR InterPro; IPR030381; G_DYNAMIN_dom.
DR InterPro; IPR027094; Mitofusin_fam.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10465; TRANSMEMBRANE GTPASE FZO1; 1.
DR PANTHER; PTHR10465:SF0; TRANSMEMBRANE GTPASE MARF-RELATED; 1.
DR Pfam; PF00350; Dynamin_N; 1.
DR Pfam; PF04799; Fzo_mitofusin; 1.
DR SUPFAM; SSF111479; Fzo-like conserved region; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51718; G_DYNAMIN_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00022787};
KW Reference proteome {ECO:0000313|Proteomes:UP000230233};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 618..638
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 644..661
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 97..352
FT /note="Dynamin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51718"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 390..417
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 775 AA; 87697 MW; 5D5AD7E73C5CB214 CRC64;
MSGTASLVHN LPASGDSNHR GLHSLKNSRR VADNEPLLRF REAKKVLGDV YGELKDNVAE
LEGVYKDIKE NDFVSAEQRE EIEAIRDSIK TIMDTFQRDN MKVVFFGRTS NGKSTTINAM
LHEKVLPQGM GHTTCCFLQV EGSEDEVGHL QLDDNPQKID MKMLGKIGHA LSDENSDLPA
MGQDSLLRVF HPKQTESGEC RLLQNDVVIL DSPGVDLSPE FDSWIDKHCL DADVFVLVSN
AESTLTQAEK NFFLRVAKKL SKPNVFILNN RWDASAAETE NIEDVKKQHL TRFRQFLVDE
LEVCSEREVN DRIFFVSSRE VLESRLKARG LVQKAYQAEG HGTRALEFQN FERHFEQCIS
RSAIHTKFEA HNRRAHEMIG KMRLNLNSVL TSAAEQRSKL QNELNEATRT FNECRVNFTQ
FEKAYREQTE QLRAEVHLKV SADFFEEIAR LDAIIDRFDQ PFDGSSSGMA KYKQDLAIFV
DKCLSSDLEA RCTGGLMSRI WNLENDMFQY VTKILAEPYQ NKLEEVWRYR APFKFSICVD
VPALVNDFHE DLEFRFTFGL HAMIRRIIAY RSGQPVTAIN TNLLTPLSLK AQAETKNVVR
DADASAAAEE QAMMTQMVLT SAAFLANGSL GVLVIGGIVY KAVGWRVIAV GGAAYAGLYA
WERMRWNSSA KEQHLKEQFR SHLAARMQQV STAHTHHCET QAIREMDQVF DGLKSTVGGV
HREMKNDLDT QKTQIDAVDS TIRTLGTIKG KAVFLLRNLE QFASSYLRSD SPSSP
//
