ID A0A2H3ISW6_9EURO Unreviewed; 548 AA.
AC A0A2H3ISW6;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Actin-related protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PENO1_004180 {ECO:0000313|EMBL:PCH08931.1};
OS Penicillium occitanis (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=290292 {ECO:0000313|EMBL:PCH08931.1, ECO:0000313|Proteomes:UP000218381};
RN [1] {ECO:0000313|EMBL:PCH08931.1, ECO:0000313|Proteomes:UP000218381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL100 {ECO:0000313|EMBL:PCH08931.1,
RC ECO:0000313|Proteomes:UP000218381};
RX PubMed=28951729; DOI=10.3389/fmicb.2017.01627;
RA Bravo-Ruiz G., Sassi A.H., Marcet-Houben M., Di Pietro A., Gargouri A.,
RA Gabaldon T., Roncero M.I.G.;
RT "Regulatory Mechanisms of a Highly Pectinolytic Mutant of Penicillium
RT occitanis and Functional Analysis of a Candidate Gene in the Plant Pathogen
RT Fusarium oxysporum.";
RL Front. Microbiol. 8:1627-1627(2017).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
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:PCH08931.1}.
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DR EMBL; NPFK01000005; PCH08931.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3ISW6; -.
DR STRING; 290292.A0A2H3ISW6; -.
DR OrthoDB; 1699194at2759; -.
DR Proteomes; UP000218381; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR Gene3D; 3.30.420.40; -; 2.
DR InterPro; IPR004000; Actin.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR PANTHER; PTHR11937; ACTIN; 1.
DR PANTHER; PTHR11937:SF14; ACTIN-RELATED PROTEIN 10; 1.
DR Pfam; PF00022; Actin; 2.
DR SMART; SM00268; ACTIN; 1.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR PROSITE; PS01036; HSP70_3; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000218381}.
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..442
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 548 AA; 61616 MW; C232399B9A60FF8F CRC64;
MATTESRHAS KSSISALEAA RARIRKDEQS FEPRTPPHHR NRSMVSSFGS SSSPLSSFRN
EEDAIILEMG ARSLRAGFEG ESMPMCSVGF GPEESRKIGD YRGWVKSNKG TTEEKVSSLD
AEEWVKNHEL WRMDLREVDL GLVEDKLERA VREIYNNYLL TDAGNARLVL VMPSIMPHPL
LSVVLETLFN RWRFPSITLL PSAAMVAAAA GVRAALVVDI GWAETTVTAI YEYRDIASRR
STRAMKTLMQ HMGRMLSHLN NPTQDETKKD GKISVNFEYC EEVVSRFAWC KFASEDEELN
KDVLIPSPPS PDSEYVHVPF SQFAKPVEAN FFAPGTDEHE FDDDETPIHN LVYNALLELP
PDIRGACMSR IIFVGGGSRI PGVRQRILNE VSSLVAEHGW DATRGRAVEE QRKRLQELRI
SREHKHAPEE KVGTTDEAHE ESSVDEAKEE EIDFIEQKIR RNQARNSKPF IQGQFRQVES
LGAWAGASLV TSLKIRGLVE VEREKFLRDG LASASRDLDG HHQVADRRSG VRSSVISDRS
SWTLAGWG
//
