ID A0A1Y1VAA9_9FUNG Unreviewed; 865 AA.
AC A0A1Y1VAA9;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Actin depolymerizing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=BCR36DRAFT_583117 {ECO:0000313|EMBL:ORX51049.1};
OS Piromyces finnis.
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC Neocallimastigaceae; Piromyces.
OX NCBI_TaxID=1754191 {ECO:0000313|EMBL:ORX51049.1, ECO:0000313|Proteomes:UP000193719};
RN [1] {ECO:0000313|EMBL:ORX51049.1, ECO:0000313|Proteomes:UP000193719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=finn {ECO:0000313|Proteomes:UP000193719};
RG DOE Joint Genome Institute;
RA Haitjema C.H., Gilmore S.P., Henske J.K., Solomon K.V., De Groot R.,
RA Kuo A., Mondo S.J., Salamov A.A., Labutti K., Zhao Z., Chiniquy J.,
RA Barry K., Brewer H.M., Purvine S.O., Wright A.T., Boxma B., Van Alen T.,
RA Hackstein J.H., Baker S.E., Grigoriev I.V., O'Malley M.A.;
RT "Genomes of anaerobic fungi encode conserved fungal cellulosomes for
RT biomass hydrolysis.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ORX51049.1, ECO:0000313|Proteomes:UP000193719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=finn {ECO:0000313|Proteomes:UP000193719};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (AUG-2016) 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:ORX51049.1}.
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DR EMBL; MCFH01000019; ORX51049.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1VAA9; -.
DR STRING; 1754191.A0A1Y1VAA9; -.
DR EnsemblFungi; ORX51049; ORX51049; BCR36DRAFT_583117.
DR OrthoDB; 101008at2759; -.
DR Proteomes; UP000193719; Unassembled WGS sequence.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR CDD; cd11961; SH3_Abp1_fungi_C2; 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; 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:UP000193719};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 3..130
FT /note="ADF-H"
FT /evidence="ECO:0000259|PROSITE:PS51263"
FT DOMAIN 731..791
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 807..865
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 182..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..225
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..343
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..364
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..479
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 480..571
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..620
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..665
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..722
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 865 AA; 96251 MW; 883DBBD990DFA228 CRC64;
MSLLYTHSRE LNASLNELKE PSSNTDWILF GYEGDDITLI NSGSNGLSEI KDEFDEECVQ
YALLKIFDET SKMLRYIYIA WCGEYAPPFQ KANFSQHSQI IENFFKGYHV KINARCYEDV
EPENIINKVQ NSSFINFSAK VAPVPFKKPM INLPNKPANP QLQKLPTPNQ LKNMEPTQTF
KLGIKKPESK PVPNTTVNPD PTPVSKAPSA APVPRPNPLN PRANPLAPRA NPLAPKQNYS
SPAPVTASKP TPAASTTTTT TNPISPQPTR ANPLSPQPNR ANPLSPQPNR ANPLSPQPTR
ANPLSPQPTR ANPLSPQPAR ANPLSPQPAR ANPLSPQPTR ANPLSPKPIR SNPLNKNAPT
TEPTFYKTAD VPRVNVSTGV FDNVKIEPTS EPAVENDSID TTARESVANV RKMFEQKPEK
KINKITLKSA FFDNQSTNNY SAQRKVREER LRREQEDNAL REREKLANQQ RELQDEISET
RKSNPLNSPK STPVTITKTN PLNNSLLFSA PKSNPLNANS SSTPITISEN NPFNTNKMNP
LNTRANPLSP PKSNPLNTRA NPLSPPKSNP LNIRANPLAP PALPERDTPP ALPQRENPLA
PPPLPQRENP LAPPALPQRA NPLAPTALPQ RANPLAPPAL PQRENPLAPP PLPARENPLA
PPPLPQRVLD SGKEKKEQEE RERKEREERE RKEREERERK EREERERKER EERERKEREQ
NNTRPSISGS NNNDSAIVSY DYEPQEENEI ALVEGEIIKN IIQLDEGWWQ GENSKGEIGL
FPSNYVELMP AASVASTPAP APAPVANNTP SAIALYDYDA QEDNEITFKE GDIITNLNFV
TDDWWEGVVN GKCGLFPGNY VEVNK
//
