ID A0A0F4Z5C0_TALEM Unreviewed; 810 AA.
AC A0A0F4Z5C0;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Actin binding protein {ECO:0000313|EMBL:KKA25724.1};
GN ORFNames=T310_0280 {ECO:0000313|EMBL:KKA25724.1};
OS Rasamsonia emersonii CBS 393.64.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Rasamsonia.
OX NCBI_TaxID=1408163 {ECO:0000313|EMBL:KKA25724.1, ECO:0000313|Proteomes:UP000053958};
RN [1] {ECO:0000313|EMBL:KKA25724.1, ECO:0000313|Proteomes:UP000053958}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 393.64 {ECO:0000313|EMBL:KKA25724.1,
RC ECO:0000313|Proteomes:UP000053958};
RA Heijne W.H., Fedorova N.D., Nierman W.C., Vollebregt A.W., Zhao Z., Wu L.,
RA Kumar M., Stam H., van den Berg M.A., Pel H.J.;
RL Submitted (APR-2015) 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:KKA25724.1}.
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; LASV01000014; KKA25724.1; -; Genomic_DNA.
DR RefSeq; XP_013332336.1; XM_013476882.1.
DR AlphaFoldDB; A0A0F4Z5C0; -.
DR STRING; 1408163.A0A0F4Z5C0; -.
DR GeneID; 25312335; -.
DR OrthoDB; 101008at2759; -.
DR Proteomes; UP000053958; Unassembled WGS sequence.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR CDD; cd11281; ADF_drebrin_like; 1.
DR CDD; cd11962; SH3_Abp1_fungi_C1; 1.
DR CDD; cd11961; SH3_Abp1_fungi_C2; 1.
DR Gene3D; 3.40.20.10; Severin; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 2.
DR InterPro; IPR035719; Abp1_fungi_SH3_C1.
DR InterPro; IPR035718; Abp1_fungi_SH3_C2.
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:UP000053958};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 3..156
FT /note="ADF-H"
FT /evidence="ECO:0000259|PROSITE:PS51263"
FT DOMAIN 653..713
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 752..810
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 169..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 322..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 716..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..380
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..496
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 564..581
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 810 AA; 86362 MW; 87F967C3F62CF001 CRC64;
MASLNLSSNG PSISRSYQSI VNAPAPSGPA ASSSTYGQWV VFSVSTPLVN AFQPDSGGKE
SVLKVQSTGE GELTDLIEEF SEGKIQFAFV KVKDPNTSLP KNVLIGWCGE GVPERTKGYF
TSHLAAVSKF LHGYHVQITA RSEGDLTPEG ILQKVADASG AKYASEETVS SGNAASKPPV
ATKPVFTPSR SAGIVSKPTT SARRTVAPKN DEVDEDGWGP DAPPVTRTQL EKVPSAYQPT
KVDIHQLTSQ KPAESTFKST QPDNNARSDI VKGGYQPVGK VDIAAIRRQA REAGEQVDDR
PEPVKGAYEP VGKVDIAALR AKAQSTDVPS PGTDDSQRVS EPKTLSERSA AFQTSERLTT
LPKPKVSNRF AVSSTFTGTK PPLPGDFGAK VTPAVAPVGG ASRTFADEGG KTPAQLWAER
KAKERGSSGA GDVPISRPSA PTQSSEREWK SSYTGRTWAP VQTTHTGLST GSNASQQPAG
HGDELSQESE SKPPSGAVSS VRDRFAPSPS VGASVSNVGE RAPSPPPLDN STKPNAGRGI
PIPGLSTGPV ESQEAYETET KQDVPNPPPQ PRSPTPPTPS HKESSPIRVA MPVSRNAPEE
IVRGAPEEQH SPPQVLPIRS LEQAVPKEEE LEEPTHDTAR ATAEATVHDT AHPNSIRALV
QYDYEKAEDN EIDLKEGEYV TEIEMVDKDW WLGVNARGER GLFPSNYVEV VEAGDATQGA
TSDLPGHEKR ETDIEASRPV GEPPATGLHS ESRGPTATAL YDYEAAEDNE ISFPEGAKII
NIEFPDEDWW SGEYDGKIGL FPANYVQLDE
//
