ID A0AAE8SYC7_9PEZI Unreviewed; 850 AA.
AC A0AAE8SYC7;
DT 29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2024, sequence version 1.
DT 28-JAN-2026, entry version 7.
DE RecName: Full=Cofilin {ECO:0000256|ARBA:ARBA00015630};
DE AltName: Full=Actin-depolymerizing factor 1 {ECO:0000256|ARBA:ARBA00032427};
GN ORFNames=DNG_08432 {ECO:0000313|EMBL:SPO05745.1};
OS Cephalotrichum gorgonifer.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Microascales; Microascaceae; Cephalotrichum.
OX NCBI_TaxID=2041049 {ECO:0000313|EMBL:SPO05745.1, ECO:0000313|Proteomes:UP001187682};
RN [1] {ECO:0000313|EMBL:SPO05745.1}
RP NUCLEOTIDE SEQUENCE.
RA Guldener U.;
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000256|ARBA:ARBA00004109}.
CC -!- SIMILARITY: Belongs to the actin-binding proteins ADF family.
CC {ECO:0000256|ARBA:ARBA00006844}.
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:SPO05745.1}.
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; ONZQ02000013; SPO05745.1; -; Genomic_DNA.
DR AlphaFoldDB; A0AAE8SYC7; -.
DR Proteomes; UP001187682; Unassembled WGS sequence.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:InterPro.
DR GO; GO:1990334; C:Bfa1-Bub2 complex; IEA:InterPro.
DR GO; GO:0044732; C:mitotic spindle pole body; IEA:TreeGrafter.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR GO; GO:0030042; P:actin filament depolymerization; IEA:InterPro.
DR GO; GO:0031578; P:mitotic spindle orientation checkpoint signaling; IEA:TreeGrafter.
DR CDD; cd11286; ADF_cofilin_like; 1.
DR Gene3D; 3.40.20.10; Severin; 1.
DR InterPro; IPR002108; ADF-H.
DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR InterPro; IPR017904; ADF/Cofilin.
DR InterPro; IPR034586; Bfa1/Byr4.
DR PANTHER; PTHR35140; MITOTIC CHECK POINT PROTEIN BFA1; 1.
DR PANTHER; PTHR35140:SF1; MITOTIC CHECK POINT PROTEIN BFA1; 1.
DR Pfam; PF00241; Cofilin_ADF; 1.
DR SMART; SM00102; ADF; 1.
DR SUPFAM; SSF55753; Actin depolymerizing proteins; 1.
DR PROSITE; PS51263; ADF_H; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Reference proteome {ECO:0000313|Proteomes:UP001187682}.
FT DOMAIN 702..846
FT /note="ADF-H"
FT /evidence="ECO:0000259|PROSITE:PS51263"
FT REGION 1..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 135..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..33
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..76
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..257
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..321
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..456
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..523
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 850 AA; 93351 MW; 67234DC843DAA2A6 CRC64;
MEPLRLKPRL PAEPAPEIEN WDDDDFFADD GDDFAFRSSI NSNPTTDRRD SMSSRRSMRS
ELESLHEEER QIHVPGDDEN STMNAITVAA NLGIPIPKNV PPSALMGGTI KRLGGRKIKK
IIDDDWDADL ELPEGGKPLA IKPQDGSRFP DAIRQVSGGS VQLSPTGSRK QASPVIHQHN
FDLGQPRSSP TGASINLDRF RDDDDDDDFF GDGSATIKVS KSRGLGKPIS LLTPPTPQKG
NGILPPTDDD FEQDLELPSD GKLKLSTTKD IPKTPALSLD DLDWGEGSLG TRYGGTRRDG
RSNRSSSASA LSPSISSSIT AESEDETFDG LVLPAGPVNF EQRLKLRRKS RSPERIPEDE
PAPQPKKLPE AEEEDFLTGL DLGESAVPRH QRAFGDGNEL DGFDDLPVSR DTEARFVKQP
VAKDVRPPLR NKIYQNVLPD RSSAASPVSP YSPVRPDYTP SFARDTAASR IAREASLAQR
APAQGPLAPL TAQRVAQLST RSNLSPNLPQ SPVRSRKHSK KQPQLKPHLI SNLNSTRDVK
ALNGMTYNPA TFKWEGNENV LGAFDPPASS PSTTSLPPYM LRERENSTPR PALIANVGST
KGVQVVGEMV FDPQNMCWLK LGASAKPVSE TGDPLDGFNG LEDDDEDVFK DIPDLEEKTT
ASNDGGAGRV SDIRDDWLVG EEFDVGPEFI RRQREEEERW RKKASVATEC VSTYNDLKLS
KKYKFIIFKL SDDNREIVVE EASDNADWEV FREKLINATT KTRSGAVGKG PRYAVYDFEY
TLATGEGVRN KITFIAWSPD DAGVQSKMIY ASSKESLKRS LTGLAVELQA NDSDDIEYDT
VLKTVSKGLA
//
