ID A0A0A8L8M0_9SACH Unreviewed; 607 AA.
AC A0A0A8L8M0;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=WGS project CCBQ000000000 data, contig 00015 {ECO:0000313|EMBL:CDO95401.1};
GN ORFNames=KLDO_g3644 {ECO:0000313|EMBL:CDO95401.1};
OS Kluyveromyces dobzhanskii CBS 2104.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=1427455 {ECO:0000313|EMBL:CDO95401.1, ECO:0000313|Proteomes:UP000031516};
RN [1] {ECO:0000313|EMBL:CDO95401.1, ECO:0000313|Proteomes:UP000031516}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS2104 {ECO:0000313|Proteomes:UP000031516};
RA Nystedt B., Astrom S.;
RT "The genome of Kluyveromyces dobzhanskii.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CDO95401.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CCBQ010000045; CDO95401.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A8L8M0; -.
DR OrthoDB; 2025446at2759; -.
DR Proteomes; UP000031516; Unassembled WGS sequence.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IEA:UniProt.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:UniProt.
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 Pfam; PF07653; SH3_2; 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 SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 5..263
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 545..607
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 270..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 125..159
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 274..312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 607 AA; 69433 MW; BA0E1F6EA3A3E01C CRC64;
MAQIYNYQES FWDEDDQGVT ILLQHVGRGI CTCELLLDSF TRRSELELDY ARRLGAISSK
IVSNLERYAD YNSMSESLKY FQSSQQRVAN GHSKAYERLN RENVGTMGDF LKQYRARWST
LTSNVENLRK LKDEKKKALK ALDQELLGAE NKLRENRLNR ETALGEYQRK ENIKELEKWS
SIVEESHRRK TVLHHEYKAA RTHWFEEWRH ISGELQDLET QRIQVSRELL QQYAEFTTQP
SELELSLMEQ LKQKLSSFTP ELEISHFSYH HGTGRIKQKS SNSVSHNNSS TKSNPSSSTR
PKPLKSVDLT KNDRYVQNVK RLSTQLKNTR LNSINALSVN KELPTPKNDA TVENHAVLKV
VDAGSALNPA ENYSEVANKD NRPTTLSESS EETCSNPTDF THRKNKSSYD SMSTSLSSMA
SSVDDSQRYA KSWNSRNRRK SRPSSMYSST ADIDTSTNSK SHHLEVPFAN RRKSIASDVE
GALKILEKND SRPMTSRTSS LASSNLTVSR TALPLNSSLN ITRCKRVTVD GEQLNLPIID
SMKNPVIRYA KATFSYTEPN DNNILLFNTE DILLLVECIN EDWYVGEVYQ GNKQHGLVPM
NYVRLIN
//