ID Q6FU67_CANGA Unreviewed; 712 AA.
AC Q6FU67;
DT 19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 116.
DE SubName: Full=Candida glabrata strain CBS138 chromosome F complete sequence {ECO:0000313|EMBL:CAG59151.1};
GN OrderedLocusNames=CAGL0F05885g {ECO:0000313|CGD:CAL0131070,
GN ECO:0000313|EMBL:CAG59151.1};
OS Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 /
OS NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces.
OX NCBI_TaxID=284593 {ECO:0000313|EMBL:CAG59151.1, ECO:0000313|Proteomes:UP000002428};
RN [1] {ECO:0000313|EMBL:CAG59151.1, ECO:0000313|Proteomes:UP000002428}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65
RC {ECO:0000313|Proteomes:UP000002428};
RX PubMed=15229592; DOI=10.1038/nature02579;
RG Genolevures;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA Wincker P., Souciet J.L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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DR EMBL; CR380952; CAG59151.1; -; Genomic_DNA.
DR RefSeq; XP_446227.1; XM_446227.1.
DR AlphaFoldDB; Q6FU67; -.
DR STRING; 284593.Q6FU67; -.
DR EnsemblFungi; CAGL0F05885g-T; CAGL0F05885g-T-p1; CAGL0F05885g.
DR GeneID; 2887667; -.
DR KEGG; cgr:CAGL0F05885g; -.
DR CGD; CAL0131070; CAGL0F05885g.
DR VEuPathDB; FungiDB:CAGL0F05885g; -.
DR eggNOG; KOG2398; Eukaryota.
DR HOGENOM; CLU_434790_0_0_1; -.
DR InParanoid; Q6FU67; -.
DR OMA; RFAKSWN; -.
DR Proteomes; UP000002428; Chromosome F.
DR GO; GO:0000142; C:cellular bud neck contractile ring; IEA:EnsemblFungi.
DR GO; GO:0000144; C:cellular bud neck septin ring; IEA:EnsemblFungi.
DR GO; GO:0044697; C:HICS complex; IEA:EnsemblFungi.
DR GO; GO:0120155; C:MIH complex; IEA:EnsemblFungi.
DR GO; GO:0051015; F:actin filament binding; IEA:EnsemblFungi.
DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR GO; GO:0032038; F:myosin II heavy chain binding; IEA:EnsemblFungi.
DR GO; GO:0005543; F:phospholipid binding; IEA:EnsemblFungi.
DR GO; GO:0051017; P:actin filament bundle assembly; IEA:EnsemblFungi.
DR GO; GO:1903475; P:mitotic actomyosin contractile ring assembly; IEA:EnsemblFungi.
DR GO; GO:1902404; P:mitotic actomyosin contractile ring contraction; IEA:EnsemblFungi.
DR GO; GO:0051126; P:negative regulation of actin nucleation; IEA:EnsemblFungi.
DR GO; GO:0090339; P:negative regulation of formin-nucleated actin cable assembly; IEA:EnsemblFungi.
DR GO; GO:0031671; P:primary cell septum biogenesis; IEA:EnsemblFungi.
DR GO; GO:0072741; P:protein localization to cell division site; IEA:EnsemblFungi.
DR GO; GO:1903471; P:regulation of mitotic actomyosin contractile ring contraction; IEA:EnsemblFungi.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR23065:SF7; CYTOKINESIS PROTEIN 2; 1.
DR PANTHER; PTHR23065; PROLINE-SERINE-THREONINE PHOSPHATASE INTERACTING PROTEIN 1; 1.
DR Pfam; PF00611; FCH; 1.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS50002; SH3; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|PROSITE-ProRule:PRU01077, ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000002428};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 1..260
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 642..710
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 271..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 322..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 522..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 598..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 135..193
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 282..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..412
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..568
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 712 AA; 80615 MW; AA05A0945974F55C CRC64;
MSYSYDTCFW DPNDNGVNVL LEHVGNGIKS MDGLTTFFKL RAELEKDYAR RLGAAIDLYD
KSYCEEYGAL FKTIQSFFPL ERSRALAHSK LSELVYRQVY SELKSLQSEL SARLTTLSGR
IEKLRFDKYD KKKGCESLSV KLRDAEVRLS ELNLNKNNII GNRRKIESLE KEQKKWESNV
HEFQIQLNVL KQEYKASQKF WINEWHSLSH DLQHLEIKRI STIQVLLQSF AQTAIDTSII
EQTKMETLIN ELATFTPMDD ISKFSSEFGT GRLKEKRQRS SRLVNGNTST ASKPSMEILS
SSHMSRGPDP YVENIRKLSS QLQKTTVTPR VLKVSRTEGT DNGKSYRAES NDYQMLNSSA
SIEHRPSSFI PSSSEPYSNS NGRNTNETLR RRVHEDKEDR RVSDHLRVGC QPKSIEREPS
FVKNIEKSAS ESGSYSSGRH SFSPSSSSGT SSNPTDFSHK IKSHRSMDSL ATSVSSMASS
IDDSQRFAKS WNSANRKRKS MSHLQSPEIN ISTIDDQLEN SKNTTAQRTT HPSQSTNTFN
RDVSSNTILV DPRYQSSKNS MDMSRVRSSR SIDSSRRKSM VLDSSVNPIS DALNEMERIK
SGGSSTAYSD EARRKDLPSG YGRVDDNGMP VTLPTITKEG EEVIKFAKAL YPLINSEAQE
LANFEKGDYL LLTEVVNEDW YRGEVYGNSN TTTTHGNGLI PSNFIQILHN QL
//
