ID S7Q2M9_MYOBR Unreviewed; 367 AA.
AC S7Q2M9;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=Septin {ECO:0000256|PIRNR:PIRNR006698};
GN ORFNames=D623_10014473 {ECO:0000313|EMBL:EPQ17538.1};
OS Myotis brandtii (Brandt's bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=109478 {ECO:0000313|EMBL:EPQ17538.1, ECO:0000313|Proteomes:UP000052978};
RN [1] {ECO:0000313|Proteomes:UP000052978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23962925; DOI=10.1038/ncomms3212;
RA Seim I., Fang X., Xiong Z., Lobanov A.V., Huang Z., Ma S., Feng Y.,
RA Turanov A.A., Zhu Y., Lenz T.L., Gerashchenko M.V., Fan D., Hee Yim S.,
RA Yao X., Jordan D., Xiong Y., Ma Y., Lyapunov A.N., Chen G., Kulakova O.I.,
RA Sun Y., Lee S.G., Bronson R.T., Moskalev A.A., Sunyaev S.R., Zhang G.,
RA Krogh A., Wang J., Gladyshev V.N.;
RT "Genome analysis reveals insights into physiology and longevity of the
RT Brandt's bat Myotis brandtii.";
RL Nat. Commun. 4:2212-2212(2013).
CC -!- FUNCTION: Filament-forming cytoskeletal GTPase.
CC {ECO:0000256|PIRNR:PIRNR006698}.
CC -!- SUBUNIT: Septins polymerize into heterooligomeric protein complexes
CC that form filaments. {ECO:0000256|PIRNR:PIRNR006698}.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. Septin GTPase family.
CC {ECO:0000256|PIRNR:PIRNR006698, ECO:0000256|RuleBase:RU004560}.
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DR EMBL; KE164370; EPQ17538.1; -; Genomic_DNA.
DR AlphaFoldDB; S7Q2M9; -.
DR eggNOG; KOG2655; Eukaryota.
DR Proteomes; UP000052978; Unassembled WGS sequence.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR CDD; cd01850; CDC_Septin; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR030379; G_SEPTIN_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR016491; Septin.
DR PANTHER; PTHR18884; SEPTIN; 1.
DR PANTHER; PTHR18884:SF6; SEPTIN-1; 1.
DR Pfam; PF00735; Septin; 1.
DR PIRSF; PIRSF006698; Septin; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51719; G_SEPTIN; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00023212, ECO:0000256|PIRNR:PIRNR006698};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212,
KW ECO:0000256|PIRNR:PIRNR006698};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|PIRSR:PIRSR006698-
KW 2};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR006698-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000052978}.
FT DOMAIN 22..296
FT /note="Septin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51719"
FT REGION 348..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 144
FT /note="Important for dimerization"
FT /evidence="ECO:0000256|PIRSR:PIRSR006698-2"
SQ SEQUENCE 367 AA; 41994 MW; 9F2FE91ECCB1CE6D CRC64;
MDKEYVGFAA LPNQLHRKSI KKGFDFTLMV AGESGLGKST LINSLFLTNL YEDRQLPEAS
ARLTQTLTIE RRGVEIEEGG IKVKLTLVDT PGFGDSVDCS DCWLPVVRFI EEQFEQYLRD
ESGLNRKNIQ DSRVHCCLYF ISPFGRGLRP LDVAFLRAVH EKVNIVPVIG KADALMPSET
QALKQKIRDQ LKEEEINIYQ FPDCDSDEDE DFKRQDAEMK ESIPFAVVGS CEVVRDKGTR
PVRGRRYSWG TVEVENPQHC DFLNLRRMLV QTHLQDLKEV THDLLYEGYR ARCLQSLARP
GARDRASRSK LSRRSTAEIP LPMLPLAETE KLIREKDEEL RRMQEMLEKM QAQVQQSQAQ
GEQSAAL
//
