ID A0A371CU95_9APHY Unreviewed; 640 AA.
AC A0A371CU95;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:RDX43863.1};
GN ORFNames=OH76DRAFT_1487535 {ECO:0000313|EMBL:RDX43863.1};
OS Polyporus brumalis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Polyporus.
OX NCBI_TaxID=139420 {ECO:0000313|EMBL:RDX43863.1, ECO:0000313|Proteomes:UP000256964};
RN [1] {ECO:0000313|EMBL:RDX43863.1, ECO:0000313|Proteomes:UP000256964}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRFM 1820 {ECO:0000313|EMBL:RDX43863.1,
RC ECO:0000313|Proteomes:UP000256964};
RX PubMed=30061923; DOI=10.1186/s13068-018-1198-5;
RA Miyauchi S., Rancon A., Drula E., Hage H., Chaduli D., Favel A., Grisel S.,
RA Henrissat B., Herpoel-Gimbert I., Ruiz-Duenas F.J., Chevret D., Hainaut M.,
RA Lin J., Wang M., Pangilinan J., Lipzen A., Lesage-Meessen L., Navarro D.,
RA Riley R., Grigoriev I.V., Zhou S., Raouche S., Rosso M.N.;
RT "Integrative visual omics of the white-rot fungus Polyporus brumalis
RT exposes the biotechnological potential of its oxidative enzymes for
RT delignifying raw plant biomass.";
RL Biotechnol. Biofuels 11:201-201(2018).
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DR EMBL; KZ857458; RDX43863.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A371CU95; -.
DR STRING; 139420.A0A371CU95; -.
DR Proteomes; UP000256964; 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; 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; PF14604; SH3_9; 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:UP000256964};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 4..132
FT /note="ADF-H"
FT /evidence="ECO:0000259|PROSITE:PS51263"
FT DOMAIN 482..543
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 581..640
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 164..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..242
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..341
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..396
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..426
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..460
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..570
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 640 AA; 67052 MW; E70AFF2DBC0121FF CRC64;
MSLQINLASR DLAQAYEDVV NARGIDWAIF TYDKGTNDLK VQATGDGGLE ELQEEFSDGR
IQYAFARVKD PNSELPKFVQ INWCGDGVPV ARKGLFHSHS SGVANFLRGT HVVINARNEA
DVEPSLIMKR VEAASGVHYS AQKEAPRKFE PIAPVGSSYK PIGRPDIAGL RSAAPPAPAA
SKPSVASAPR SVPPAPSSAP APGKVTVANK APVDAWADEG DSFAPPPPPP AASRPTPSAP
KAAPSQPAAR FTPAAHTPVA ASNVPTKPAE EDKIGPVGTN YTPIKLQPKK LVNPFAAKES
QTQAESAAPK PSPAGGAKKL TWSERQALAK KQQEEEEARA EAALGSQPTP SAPSFRGGVP
PPPRMPAMHP PPAAAEEPEE EYTPPPPPPA PPAVPSANRP ARAASPVVEA AAPPPPPPPP
PPAVAQHEAE PEWETEAAPP PPPPPPPPPP PPGAPVAARE PEPEPEPEPA PAPAPAAAHA
QGQGICAIVQ YSYEAQEDNE MDLIEGELIE QIEQLDEGWW SGVSADGSKQ GLFPANYVEI
VEQEAKSATP PPPSPPPPPP PPPPPAAPAV AAQLEPEAEE DLGSWAVAIY DYDASEDNEI
SFKEGDRITH IEAASEDWWQ GTDKDGNVGL FPANYVELQG
//
