(data stored in ACNUC7421 zone)

SWISSPROT: Q4WNG0_ASPFU

ID   Q4WNG0_ASPFU            Unreviewed;       363 AA.
AC   Q4WNG0;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   11-DEC-2019, entry version 107.
DE   RecName: Full=Actin-related protein 2/3 complex subunit {ECO:0000256|PIRNR:PIRNR038093};
GN   ORFNames=AFUA_6G06500 {ECO:0000313|EMBL:EAL88504.1};
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=330879 {ECO:0000313|EMBL:EAL88504.1, ECO:0000313|Proteomes:UP000002530};
RN   [1] {ECO:0000313|EMBL:EAL88504.1, ECO:0000313|Proteomes:UP000002530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100
RC   {ECO:0000313|Proteomes:UP000002530};
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.,
RA   Fedorova N., Fedorova N., Feldblyum T.V., Fischer R., Fosker N., Fraser A.,
RA   Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B., Haas H., Harris D., Horiuchi H.,
RA   Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K.,
RA   Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafon A., Latge J.P.,
RA   Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y.,
RA   Molina M., Monod M., Mouyna I., Mulligan S., Murphy L., O'Neil S.,
RA   Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA   Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H.,
RA   Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M.,
RA   Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D.,
RA   Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G.,
RA   Vazquez de Aldana C.R., Weidman J., White O., Woodward J., Yu J.H.,
RA   Fraser C., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.,
RA   Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
CC   -!- FUNCTION: Functions as component of the Arp2/3 complex which is
CC       involved in regulation of actin polymerization and together with an
CC       activating nucleation-promoting factor (NPF) mediates the formation of
CC       branched actin networks. {ECO:0000256|PIRNR:PIRNR038093}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, actin patch
CC       {ECO:0000256|PIRNR:PIRNR038093}.
CC   -!- SIMILARITY: Belongs to the WD repeat ARPC1 family.
CC       {ECO:0000256|PIRNR:PIRNR038093}.
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:EAL88504.1}.
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DR   EMBL; AAHF01000006; EAL88504.1; -; Genomic_DNA.
DR   RefSeq; XP_750542.1; XM_745449.1.
DR   STRING; 746128.CADAFUBP00007050; -.
DR   EnsemblFungi; EAL88504; EAL88504; AFUA_6G06500.
DR   GeneID; 3508154; -.
DR   KEGG; afm:AFUA_6G06500; -.
DR   EuPathDB; FungiDB:Afu6g06500; -.
DR   HOGENOM; HOG000181752; -.
DR   InParanoid; Q4WNG0; -.
DR   KO; K05757; -.
DR   OMA; FNTFRNA; -.
DR   OrthoDB; 848569at2759; -.
DR   Proteomes; UP000002530; Chromosome 6.
DR   GO; GO:0030479; C:actin cortical patch; IEA:UniProtKB-SubCell.
DR   GO; GO:0005885; C:Arp2/3 protein complex; IBA:GO_Central.
DR   GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR   GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; IBA:GO_Central.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR017383; ARPC1.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   PANTHER; PTHR10709; PTHR10709; 1.
DR   Pfam; PF00400; WD40; 2.
DR   PIRSF; PIRSF038093; ARP2/3_su1; 1.
DR   SMART; SM00320; WD40; 5.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 1.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q4WNG0.
DR   SWISS-2DPAGE; Q4WNG0.
KW   Actin-binding {ECO:0000256|PIRNR:PIRNR038093};
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR038093};
KW   Cytoskeleton {ECO:0000256|PIRNR:PIRNR038093};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002530};
KW   WD repeat {ECO:0000256|PROSITE-ProRule:PRU00221}.
FT   DOMAIN          50..91
FT                   /note="WD_REPEATS_REGION"
FT                   /evidence="ECO:0000259|PROSITE:PS50294"
FT   REPEAT          50..82
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
SQ   SEQUENCE   363 AA;  39984 MW;  FD3D4CA4004B5CD2 CRC64;
     MSAPEVHHLF HSPIADHSFS SDKSTLAVAR ENNVELYQRT GNKFSLTDEL KGHEKTVTSV
     DIAPNSGRIV TCSQDRNAYV WEQTPTGWKP TLVLLRINRA ATFVRWSPSE QKFAVGSGAR
     VIAVCYFEEE NDWWISKHLK KPIRSTITTL SWHPNSVLLA AGSTDSHARV FSSFIKGIDT
     RPEPSAWGER LPFNTVCGEF LNDSAGWIHA VCFSPSGNAL AFTGHDSSVT VVYPSAPEQP
     PRAMLNITTR LLPFTSLIWN GENEIIAAGH DCEPFRFSGD ESGWKLAGAI ESKTGAGAGS
     VRDESALNMF RQMDLKGQTH ADTQLKTIHQ NTINTIRVYK ETGGAVHQFS TSGVDGRVVV
     WTI
//

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