ID A0A1V6YQX7_PENNA Unreviewed; 691 AA.
AC A0A1V6YQX7;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 13-SEP-2023, entry version 22.
DE RecName: Full=Actin-like ATPase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PENNAL_c0013G00522 {ECO:0000313|EMBL:OQE89826.1};
OS Penicillium nalgiovense.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=60175 {ECO:0000313|EMBL:OQE89826.1, ECO:0000313|Proteomes:UP000191691};
RN [1] {ECO:0000313|Proteomes:UP000191691}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 13039 {ECO:0000313|Proteomes:UP000191691};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
CC -!- SIMILARITY: Belongs to the actin family.
CC {ECO:0000256|RuleBase:RU000487}.
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:OQE89826.1}.
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DR EMBL; MOOB01000013; OQE89826.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6YQX7; -.
DR STRING; 60175.A0A1V6YQX7; -.
DR OMA; RYIFEKT; -.
DR OrthoDB; 2641150at2759; -.
DR Proteomes; UP000191691; Unassembled WGS sequence.
DR Gene3D; 3.30.420.40; -; 3.
DR Gene3D; 3.90.640.60; -; 1.
DR InterPro; IPR004000; Actin.
DR InterPro; IPR043129; ATPase_NBD.
DR PANTHER; PTHR11937; ACTIN; 1.
DR PANTHER; PTHR11937:SF451; ACTIN-LIKE PROTEIN ARP9; 1.
DR Pfam; PF00022; Actin; 1.
DR SMART; SM00268; ACTIN; 1.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000191691}.
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 99..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..394
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..607
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..636
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 691 AA; 74095 MW; 130F2874FB0B0B4A CRC64;
MGRKRERKSS HRGAPVRSHH SSQSSQRSLL PLVTMPPFKD EHILLIAPGS QMTLAQLGLP
ETFTPARFRF PTRMFPAEKK GEYEPYRVHE RRQEVKVNND TDAPKPDVEM KDAEPATADG
TTATETTVKT DENTQDNGDS TKTIEEVFYE EDPASDEGAI YPIENGRIVD WPCFFALLTH
IHNTLSPPFH TPIMLIGQPV WSARDREAIT QFVFEKFKAP AFSLMDSALA ACYGYGTATA
TVVDVGKGKV DVTAVTDFAV NEHGRGIALE GCGGDAMTDR LVELLGPKGF TREMCEQLKR
SNITEILPQG TPLPGSAATA RQGANPAAAA STGGPDGDES APRGPGDGTQ TGIEGDNGDE
EEEGVLDVAA IVSGDPTEYL ANVEKEKTTT KKGAVDPKGA RLPNSKKEKA SFQFEEFVQL
EGEKAAANGA RQYIRHTRDI EVSVERFLLT SPRSKVGNRL TSGILEDIAT QVHHTILAVP
DATKRSELWD SLIIVGCGSK VKGFTQALLA VITQKFILSP SGTIFTSEIP SNFTTPLPTG
ANTPAPMGQP GPMYHPTAPG VNPLLVAATH NNPGMPGGMP GTPSMDPSMM SHHRSTGHSQ
TPTSVKTLKL PEYFPDFKDQ GNSNAPGTSA GGTPGVPGTS QGGHGMEEAV FLGAQMAAKV
FFVIDQGLSK GYMSRVEYNE SGPSAVHEYI L
//