GenomeNet

Database: UniProt
Entry: C4YA47_CLAL4
LinkDB: C4YA47_CLAL4
Original site: C4YA47_CLAL4 
ID   C4YA47_CLAL4            Unreviewed;       645 AA.
AC   C4YA47;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 68.
DE   RecName: Full=Actin-binding protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CLUG_04985 {ECO:0000313|EMBL:EEQ40857.1};
OS   Clavispora lusitaniae (strain ATCC 42720) (Yeast) (Candida lusitaniae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Metschnikowiaceae; Clavispora.
OX   NCBI_TaxID=306902 {ECO:0000313|EMBL:EEQ40857.1, ECO:0000313|Proteomes:UP000007703};
RN   [1] {ECO:0000313|EMBL:EEQ40857.1, ECO:0000313|Proteomes:UP000007703}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42720 {ECO:0000313|EMBL:EEQ40857.1,
RC   ECO:0000313|Proteomes:UP000007703};
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA   Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA   Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA   Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA   Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA   Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA   Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
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; CH408081; EEQ40857.1; -; Genomic_DNA.
DR   RefSeq; XP_002614970.1; XM_002614924.1.
DR   AlphaFoldDB; C4YA47; -.
DR   STRING; 306902.C4YA47; -.
DR   GeneID; 8495655; -.
DR   KEGG; clu:CLUG_04985; -.
DR   VEuPathDB; FungiDB:CLUG_04985; -.
DR   HOGENOM; CLU_459326_0_0_1; -.
DR   InParanoid; C4YA47; -.
DR   OMA; FKEPRGA; -.
DR   OrthoDB; 101008at2759; -.
DR   Proteomes; UP000007703; Unassembled WGS sequence.
DR   GO; GO:0003779; F:actin binding; IEA:InterPro.
DR   CDD; cd11281; ADF_drebrin_like; 1.
DR   CDD; cd11819; SH3_Cortactin_like; 1.
DR   Gene3D; 3.40.20.10; Severin; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 2.
DR   InterPro; IPR002108; ADF-H.
DR   InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR10829; CORTACTIN AND DREBRIN; 1.
DR   PANTHER; PTHR10829:SF25; DREBRIN-LIKE PROTEIN; 1.
DR   Pfam; PF00241; Cofilin_ADF; 1.
DR   Pfam; PF00018; SH3_1; 2.
DR   PRINTS; PR00499; P67PHOX.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00102; ADF; 1.
DR   SMART; SM00326; SH3; 2.
DR   SUPFAM; SSF55753; Actin depolymerizing proteins; 1.
DR   SUPFAM; SSF50044; SH3-domain; 2.
DR   PROSITE; PS51263; ADF_H; 1.
DR   PROSITE; PS50002; SH3; 2.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000007703};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          5..133
FT                   /note="ADF-H"
FT                   /evidence="ECO:0000259|PROSITE:PS51263"
FT   DOMAIN          501..562
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          586..645
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          141..510
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          559..592
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        255..273
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        276..291
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        298..314
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        358..383
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        385..408
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        458..472
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        486..510
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   645 AA;  70083 MW;  155402CE333371F5 CRC64;
     MEKIDLSTNS KHIQDSYNKV VRGDGSTTYA VFSVDKNGVL DATASGSGDL SEFVEEFTDG
     HVQFGLARVS VPGSDVFKNL LLGWCPDNAP VKLRMSFASN FADVSRVLSG YHVQITARDQ
     DDLDVDEFVA RVAAAAGANY SAQTLGKTQK STPKPAPAAV KPAPAAKPAP VAAKKPASFV
     PKTTGKPIAP VTPKPVIPKP ASFSTKTVAK SSDNDDEWGG EKEIEERDFE RQPLESVPSA
     YKPTKVDIDS LRKQKSDTIS STPKPSLSNT AASEEKDEPA PLKDRLKAYE SNDGRLTSLP
     KPKISNSVAS RFKPAVSSGP SFGAKPTFGA PVKKEKPAGG ISRNFGSENG KTPAQLWAEK
     RGKYKDVSAD EDLAEKTASL SVEQEPEEPE QEPEHEEPEE EPEHEEEEEE KPQQSLPSVI
     KPINSFAAPP KRNLPPAPAV KEEEEEQEEE EEAPTPSLPA RGLPPLPSRS EEPAPSLPTR
     KEEPAPSLPS RTHEEPKEEP KAGVKAVAQY DYEKDEDNEI GFAEGDLIVE IEFVDEEWWS
     GKHVKTGEVG LFPGSYVSIK EDDEEADEAP EASPKEEAAE EETPATSGNS AVAEYDYEKD
     EDNEISFAEG DLIVEIEFVD EDWWSGKNSK TGEVGLFPAN YVKLQ
//
DBGET integrated database retrieval system