ID   S9W5B6_SCHCR            Unreviewed;       850 AA.
AC   S9W5B6;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=GTPase Msp1 {ECO:0000313|EMBL:EPY53754.1};
GN   ORFNames=SPOG_03012 {ECO:0000313|EMBL:EPY53754.1};
OS   Schizosaccharomyces cryophilus (strain OY26 / ATCC MYA-4695 / CBS 11777 /
OS   NBRC 106824 / NRRL Y48691) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=653667 {ECO:0000313|EMBL:EPY53754.1, ECO:0000313|Proteomes:UP000015464};
RN   [1] {ECO:0000313|EMBL:EPY53754.1, ECO:0000313|Proteomes:UP000015464}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OY26 / ATCC MYA-4695 / CBS 11777 / NBRC 106824 / NRRL Y48691
RC   {ECO:0000313|Proteomes:UP000015464};
RX   PubMed=21511999; DOI=10.1126/science.1203357;
RA   Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA   Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA   Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA   Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA   French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA   Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA   Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA   Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA   Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA   Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT   "Comparative functional genomics of the fission yeasts.";
RL   Science 332:930-936(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; KE546988; EPY53754.1; -; Genomic_DNA.
DR   RefSeq; XP_013021127.1; XM_013165673.1.
DR   AlphaFoldDB; S9W5B6; -.
DR   STRING; 653667.S9W5B6; -.
DR   EnsemblFungi; EPY53754; EPY53754; SPOG_03012.
DR   GeneID; 25037333; -.
DR   eggNOG; KOG0446; Eukaryota.
DR   HOGENOM; CLU_008640_0_0_1; -.
DR   OMA; PLKMGYV; -.
DR   OrthoDB; 1052588at2759; -.
DR   Proteomes; UP000015464; Unassembled WGS sequence.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IEA:EnsemblFungi.
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:EnsemblFungi.
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; IPR000375; Dynamin_stalk.
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; PF01031; Dynamin_M; 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:UP000015464}.
FT   DOMAIN          207..478
FT                   /note="Dynamin-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51718"
FT   DOMAIN          752..845
FT                   /note="GED"
FT                   /evidence="ECO:0000259|PROSITE:PS51388"
FT   REGION          111..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        111..128
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   850 AA;  96618 MW;  DE3910951C64A2E4 CRC64;
     MFSEEGFHPF RAYSILKGPG ALKAFFRSLR LPIAGFSLVA GGVAYVGAQV QRASDYTKDV
     FDRSFDVVNS AWDKTREVVN DATSINLPEI HMPGWMEKIL RLDEESVENR RQLQLRKSQE
     KERQLGEKGN ESGGSGSDDN SEGVVVGLAG AVASTLATDE ENDFEKLNEE EKQKLAQSSK
     DDRMMIFTKK MIEIRNILHD IQDDNSSITL PSIVVIGSQS SGKSSVLEAI VGHEFLPKGS
     NMVTRRPIEL TLVHSKETTT PYCEFNGVQL GHITDFTKVQ QVLTDFNMAV PPRQGVDDNP
     IRLTICASHI PNLSLIDLPG YIQIHSSDQP ADLDDKISAL CDKYIQEPNI ILAVCAADVD
     LANSTALRAS RRVDPLGLRT IGVITKMDLV PPEKAVSILR NEHYPLHYGY IGVISKVPPL
     SLWSRNQNLT DIVSSRERSY FSAHPQFHDL PILPMLGIQN LRKNLIHVLE YTMSKNLQYT
     ADSIRSELDD CNYQYKVQYN DRLLTAESYI AENLDVLKAA FKELSQKFDK NEVRALLKEI
     LNEKTLDLLA ERYWMDENIL NWTKQSKATD EHWQYKLDSC VSLLTRMGLG RVSTLQVTEL
     LSRRIEEIAK QSPFGEHPGA LQYILNATQD ILRRRYHNTS EQVENCVKPY KFEVEINDEE
     WKVSRSEAQS MIQKELSMCQ NAEEKIRKAL GSKRLSQVLE FLNSQAKSPE PLPVAHSAVV
     LDQGRLMQYL QMRENILKLR LSTMKSKTCK SKESKYLCPE VFLNAVSNKL INTAVLFINI
     ELLSEFYYQF PRELDQRLIH SLTSEQLTSF VDENPRLKSQ LQLQRKKQGL ELALQKINSL
     VMLERQTDNE
//