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Database: UniProt
Entry: A5DMM3_PICGU
LinkDB: A5DMM3_PICGU
Original site: A5DMM3_PICGU 
ID   A5DMM3_PICGU            Unreviewed;       905 AA.
AC   A5DMM3;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2008, sequence version 2.
DT   24-JAN-2024, entry version 72.
DE   RecName: Full=Dynamin-type G domain-containing protein {ECO:0000259|PROSITE:PS51718};
GN   ORFNames=PGUG_04524 {ECO:0000313|EMBL:EDK40425.2};
OS   Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS   / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX   NCBI_TaxID=294746 {ECO:0000313|EMBL:EDK40425.2, ECO:0000313|Proteomes:UP000001997};
RN   [1] {ECO:0000313|EMBL:EDK40425.2, ECO:0000313|Proteomes:UP000001997}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL
RC   Y-324 {ECO:0000313|Proteomes:UP000001997};
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA   Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA   Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA   Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA   Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA   Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA   Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
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DR   EMBL; CH408159; EDK40425.2; -; Genomic_DNA.
DR   RefSeq; XP_001483794.1; XM_001483744.1.
DR   AlphaFoldDB; A5DMM3; -.
DR   STRING; 294746.A5DMM3; -.
DR   GeneID; 5125091; -.
DR   KEGG; pgu:PGUG_04524; -.
DR   VEuPathDB; FungiDB:PGUG_04524; -.
DR   eggNOG; KOG0448; Eukaryota.
DR   HOGENOM; CLU_011752_0_0_1; -.
DR   InParanoid; A5DMM3; -.
DR   OMA; RCERMIL; -.
DR   OrthoDB; 1381184at2759; -.
DR   Proteomes; UP000001997; Unassembled WGS sequence.
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:0007005; P:mitochondrion organization; IEA:UniProt.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR045063; Dynamin_N.
DR   InterPro; IPR030381; G_DYNAMIN_dom.
DR   InterPro; IPR027094; Mitofusin_fam.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR10465:SF0; SARCALUMENIN; 1.
DR   PANTHER; PTHR10465; TRANSMEMBRANE GTPASE FZO1; 1.
DR   Pfam; PF00350; Dynamin_N; 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};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001997}.
FT   DOMAIN          258..522
FT                   /note="Dynamin-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51718"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          476..500
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..30
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   905 AA;  101681 MW;  61D677AF07D6E5E1 CRC64;
     MENHEDSESP ETDNQTIHPY TNITKGPDTT KTIRFASESA TTRLPRITTM SFKGFKSFRD
     SATNDDTSTV VADEQAGANG PASVMYIPEN GDFLDDSSTL FNGVGAGKSS RPAPNRQQHL
     NASLQQLHYN ENRVALDRAI NSTVELIHEL CGENQQRPIF YPADAEDSSQ LLLNSTRAHL
     ALVRNNSTIS AKTLSKAKID AKEEDIPTFR LLKLNVKLSA NHNDNLVSTL DKSSIAALLE
     QKLNQQIKYL LNLKERVDDT SSKVFVTGDL NAGKSTFCNA LLRRKVLPED QQPCTSVFCE
     VIDAVNENRG VEEVHAVPIG AQYDIKDAST YEVHPLKELE DLVYDCDKYS LLKVYVIDNR
     SLQESLLRNG IVDIKLIDAP GLNMDSFQTT QVFSRQEEID LIVFVVNAEN HFTLSAKEFI
     AAAAAEKRYV FIVVNKFDNI KDKNKCMNKV LEQVKNLSPD TYKDAQEFVH FVSSSDFDGD
     EDPNPDDGPD NNGPNGHPDF DKLEASLRKF VLEKRALSKL LPAKNYLNNL LDDLQTLAKV
     NEKMYAVEKE DKTAELENQV APSYNKIKSK SNKAGDTLHK LIEDTCTEVY ESTKKQILNT
     VNNFGDEQIV PYHGLQYVYE YAKETQQAMV DTILSALTSC EEQAKIKTEK QVEEIVKVGQ
     ATLGEGFLQG KVFKSELMFT RRRDTIKRKI NDQIEVSDFF DPSIDSFMLW MGIPRHFTSQ
     FQAYNPVNIL SSVPSSAASL KNSIPSQLTL HTVYSSTKLL TAGALVRKMY SLTSVLNSTT
     LKKIAGPVLI GVAGFSIYYL INDIPNAFPR KQARKIKKQI QELDYSHVNA DRISKECRQV
     LNYPTRQVLN GFQTSIDKRL LEKEKLEKQI KDADLSYGYF HEMLVKISNQ KSSLASIELE
     VNIVD
//
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