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Database: UniProt
Entry: A0A1J9QCM0_9EURO
LinkDB: A0A1J9QCM0_9EURO
Original site: A0A1J9QCM0_9EURO 
ID   A0A1J9QCM0_9EURO        Unreviewed;       765 AA.
AC   A0A1J9QCM0;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Actin-like protein arp5 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AJ78_06574 {ECO:0000313|EMBL:OJD12909.1};
OS   Emergomyces pasteurianus Ep9510.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emergomyces.
OX   NCBI_TaxID=1447872 {ECO:0000313|EMBL:OJD12909.1, ECO:0000313|Proteomes:UP000182235};
RN   [1] {ECO:0000313|EMBL:OJD12909.1, ECO:0000313|Proteomes:UP000182235}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 9510 {ECO:0000313|EMBL:OJD12909.1,
RC   ECO:0000313|Proteomes:UP000182235};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C.A., Munoz J.F., Imamovic A., Priest M.E., Young S., Clay O.K.,
RA   McEwen J.G.;
RT   "Emmonsia species relationships and genome sequence.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:OJD12909.1}.
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DR   EMBL; LGRN01000353; OJD12909.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J9QCM0; -.
DR   STRING; 1447872.A0A1J9QCM0; -.
DR   OrthoDB; 196861at2759; -.
DR   Proteomes; UP000182235; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   Gene3D; 3.30.420.40; -; 2.
DR   InterPro; IPR004000; Actin.
DR   InterPro; IPR043129; ATPase_NBD.
DR   PANTHER; PTHR11937; ACTIN; 1.
DR   PANTHER; PTHR11937:SF16; ACTIN-RELATED PROTEIN 5; 1.
DR   Pfam; PF00022; Actin; 2.
DR   SMART; SM00268; ACTIN; 1.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000182235}.
FT   REGION          1..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          439..468
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          517..541
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          312..339
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..43
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        523..541
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   765 AA;  87269 MW;  EDAAA9F4DB1B1948 CRC64;
     MTITSTRLLV SPRTAADISQ RNDPKPPPKL YPIQDPPFKG YIPPQPEGYE QSRETASSSA
     IVIDNGSHLV KAGWSFDKSP RFIIPPVMAK YRDRKFNRTC HFAGYDAYVD ATTRGQVRNA
     FDPGTNIVGN WDVMEGVLDY IFLKLGVDGA NGGVDRPIVL TEPIANLGYS RKMMNEILFE
     CYSAPSVTYG IDSLFSYRYN RGTDGLVISS SHSSTHVIPV LNSKALLSSS TRLNWGGQQA
     ADYMMKLLKL KYPTFPDRMT EHQMIQVIHE HCYVSTDYDR ELSGYLDWTG LEDRDRVIQY
     PFTEHVVVEK TAEELARIAE RKKESGRRLQ EQAAKMRLEK LMKKEQELEY YRDLQQGLAS
     ESKKEVKRIL DAEDMKDEAH LERTIRELEK SIKKSRNKDL GNEETEEQEE ATFPLLDVPD
     EELDEAGIKE KRHQRLMKSN IEARQRAKAE KEMEKARQAE EERLDNEKRE NNFDEWIEER
     RQARETLLQK LKEKERLKAD LGNRKSLASQ MRMKTLANLA SDTPTKKRRR GPDDDTFGAN
     DDDWRVYRTV ATGPDGAGAG SDDDDNDELD IPAQLRAIEQ QLLQHDPLFT ENHTLDAQSD
     WTKSMIHMFL RGPWPFDPES TREAHQLHLN VERIRVPEVV FQPSAIAGLD QAGLVEIAAD
     IVNQRFSQGE ERARLLSDVF VTGGNSLFEG FDERFAKEFR TVLPVEMGPV LKVRRAGDAV
     LDAWRGAAEW ASGSEFKSAA LSRQEWLEKG GEYIKEHNLG NAGCM
//
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