ID F2Q4N6_TRIEC Unreviewed; 542 AA.
AC F2Q4N6;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE SubName: Full=Cell division control protein 3 {ECO:0000313|EMBL:EGE09104.1};
GN ORFNames=TEQG_08037 {ECO:0000313|EMBL:EGE09104.1};
OS Trichophyton equinum (strain ATCC MYA-4606 / CBS 127.97) (Horse ringworm
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=559882 {ECO:0000313|Proteomes:UP000009169};
RN [1] {ECO:0000313|Proteomes:UP000009169}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4606 / CBS 127.97 {ECO:0000313|Proteomes:UP000009169};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(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; DS995795; EGE09104.1; -; Genomic_DNA.
DR AlphaFoldDB; F2Q4N6; -.
DR VEuPathDB; FungiDB:TEQG_08037; -.
DR eggNOG; KOG2655; Eukaryota.
DR HOGENOM; CLU_017718_8_3_1; -.
DR Proteomes; UP000009169; 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:SF126; SEPTIN; 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:EGE09104.1};
KW Cell division {ECO:0000313|EMBL:EGE09104.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU004560};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004560}.
FT DOMAIN 165..440
FT /note="Septin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51719"
FT REGION 21..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 509..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..79
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..106
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 542 AA; 61294 MW; 13716683C5BB8BAD CRC64;
MEEKTVEVGL LDEKMAVMLP EIPIAEPITI LPEPEPEPEP EPEPDSGSDY TRSLETATDT
ENTTEPGVDS DKKSESETDN DPPAASNGIP TPTRPSPAPP SPHVSPHVER SNPMGHGAAQ
TVSSKDPKAA AQAASDMKNV VRRKLAGYVG FANLPNQWHR KSVRKGFNFN VMVVAGESGL
GKSTLVNTLF NTSLYPPRER TGPSLDIIPK TVSVESISAD IEENGVRLRL TVVDTPGFGD
FVNNDDSWRP IVENIEQRFD AYLDAENKVN RMNIVDNRVH ACVYFIQPTG HSLKPLDIEV
MRRLHTKVNL IPVIAKADTL TDEEIALFKQ RILADIQHHS IQIFEGPRYE LDDEETIAEN
KEIMSKVPFA VVGANSEVVS ADGRKVRGRR YPWGVIEVDN EEHCDFVKLR QMLIRTHMEE
LKEHTNNTLY ENYRSDKLTQ MGVTQDPSVF KEVNPAVKQE EERALHEQKL AKMEAEMKMV
FQQKVQEKES KLKQSEDELF ARHREMKEQL DRQRQELEEK KARLESGRPL EDKIKRKGFS
LR
//
