ID K1WKP7_MARBU Unreviewed; 494 AA.
AC K1WKP7;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE SubName: Full=Cell division control protein 12 {ECO:0000313|EMBL:EKD13446.1};
GN ORFNames=MBM_08529 {ECO:0000313|EMBL:EKD13446.1};
OS Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Drepanopezizaceae; Drepanopeziza.
OX NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD13446.1, ECO:0000313|Proteomes:UP000006753};
RN [1] {ECO:0000313|EMBL:EKD13446.1, ECO:0000313|Proteomes:UP000006753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB_m1 {ECO:0000313|EMBL:EKD13446.1,
RC ECO:0000313|Proteomes:UP000006753};
RX PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA Huang M.-R., Wu R., Zhou Y.;
RT "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT evolution.";
RL BMC Genomics 13:382-382(2012).
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. Septin GTPase family.
CC {ECO:0000256|RuleBase:RU004560}.
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DR EMBL; JH921450; EKD13446.1; -; Genomic_DNA.
DR RefSeq; XP_007296418.1; XM_007296356.1.
DR AlphaFoldDB; K1WKP7; -.
DR STRING; 1072389.K1WKP7; -.
DR GeneID; 18764464; -.
DR KEGG; mbe:MBM_08529; -.
DR eggNOG; KOG2655; Eukaryota.
DR HOGENOM; CLU_017718_8_0_1; -.
DR InParanoid; K1WKP7; -.
DR OMA; EVENPMH; -.
DR OrthoDB; 2732954at2759; -.
DR Proteomes; UP000006753; Unassembled WGS sequence.
DR GO; GO:0005938; C:cell cortex; IEA:UniProt.
DR GO; GO:0032156; C:septin cytoskeleton; IEA:UniProt.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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:SF109; SEPTIN-1; 1.
DR Pfam; PF00735; Septin; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51719; G_SEPTIN; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000313|EMBL:EKD13446.1};
KW Cell division {ECO:0000313|EMBL:EKD13446.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU004560};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004560};
KW Reference proteome {ECO:0000313|Proteomes:UP000006753}.
FT DOMAIN 28..292
FT /note="Septin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51719"
FT REGION 360..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..464
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 494 AA; 56012 MW; AE091108AAA9C72F CRC64;
MAPPSTESAS PIGIANLPNQ RHKIVAKRGA AFTLMVAGES GLGKSTWINT AHHKRRHAKQ
VDKTVEIEIT KAELEEKFFK VRLTVIDTPG FGDYVNNRDS WMPIIEFLDD QHESYMLQEQ
QPRRVDKIDL RVHACLYFIR PTGHTLKPLD IEVMKRLSSR VNLIPVVAKA DTLSPIDLAR
FKQRIRAVIE AQGIKIYTPP IEEDDEAAAQ HARSLMAAMP FAVIGSEKDV KTSDGRIVKG
RQYSWGVAEV ENEDHCDFKK LRSILIRTHM LDLIHTTEEA HYEAYRAQQM ETRKFGEARP
RKLDNPKFKE EEESLRKRFT EQVKIEEHRF RQWEQKLISE RDRLNKDLES THAAIKSLEG
ELEQMQGSAV RSHGRRRRCR IPPDYAPPTG RPSTRRRPCL AAGPCPGAGL EGGCLMSLGN
YHGQIWVEGA LPFSAVWFGR VEQRKGEEEK KKKKRKKKKK RGEVPTRRAA PAASPPSSAR
LSGSPAAATT AALY
//