ID Q6BHH1_DEBHA Unreviewed; 680 AA.
AC Q6BHH1;
DT 16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT 16-AUG-2004, sequence version 1.
DT 24-JAN-2024, entry version 107.
DE SubName: Full=DEHA2G18634p {ECO:0000313|EMBL:CAG90857.1};
GN OrderedLocusNames=DEHA2G18634g {ECO:0000313|EMBL:CAG90857.1};
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592 {ECO:0000313|EMBL:CAG90857.1, ECO:0000313|Proteomes:UP000000599};
RN [1] {ECO:0000313|EMBL:CAG90857.1, ECO:0000313|Proteomes:UP000000599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC
RC 2968 {ECO:0000313|Proteomes:UP000000599};
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; CR382139; CAG90857.1; -; Genomic_DNA.
DR RefSeq; XP_462350.1; XM_462350.1.
DR AlphaFoldDB; Q6BHH1; -.
DR STRING; 284592.Q6BHH1; -.
DR GeneID; 2905290; -.
DR KEGG; dha:DEHA2G18634g; -.
DR VEuPathDB; FungiDB:DEHA2G18634g; -.
DR eggNOG; KOG3655; Eukaryota.
DR HOGENOM; CLU_459326_0_0_1; -.
DR InParanoid; Q6BHH1; -.
DR OMA; FKEPRGA; -.
DR OrthoDB; 101008at2759; -.
DR Proteomes; UP000000599; Chromosome G.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR CDD; cd11281; ADF_drebrin_like; 1.
DR CDD; cd11819; SH3_Cortactin_like; 2.
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:UP000000599};
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 531..592
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 620..680
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 139..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 592..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..283
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..395
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..449
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..471
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..541
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 680 AA; 74332 MW; 733E8231DF19FCA9 CRC64;
MEKIDLSTNS KKIKEAYEKV VRGDPSSNYV VYTVDKNSSL EVSESGDGSL DEFIEHFEDG
SVQFGLARVI VPGSDVSKNL LVGWCPDNAP AKSRLSFANN FADVSNAFSG YHVQVTARDQ
DDLDAEEFLH RVCAAAGARY STQASSKPAP KPAASKPVVA KSSPKPAFSK PSVPKSTGKP
LSPITPKPTI PKPAAASSNN DDGWGDEKEI EERDFEKKPL ENVPSAYKPT KVDISELRKQ
KSDTISSQPN KKPFASQDKS DETSKDDDEP KSLSDRMKSF KSSDTSDGRL TSLPKPKVNH
SVASRFSPAN TSSKSPSFGS KPTLGYGSAN DNKKDKLVGG LSRNYAAEGG KTPAQLWAEK
RGQYKSVKSE EDKPTQNETS ELADKFSKSS IDDHEEDSTE ETEEPALIKP STGGFPVPPK
RSLPPRVDEP EEEQEEEQEE HEEEEDDEKP VEPPIIKPST GAFPTPPKRN LPPRAEEPEE
EEEEEEVEKE ETKAAPVPSL PARNLPPPPA RTTEPKQEDV APTSKHTEEK SEVITAVAEY
DYEKDEDNEI EFAEGDLITE IEFVDEEWWS GKHSTTGDVG LFPASYVSLQ NDSGKEASTT
VGKTSAPETS STPSGSADAN KGPSATAEYD YEKDEDNEIS FAEGDKIVEI EFIDEDWWSG
KHSSSGEVGL FPANYVKLDQ
//
