ID Q4WGA3_ASPFU Unreviewed; 688 AA.
AC Q4WGA3;
DT 05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 110.
DE SubName: Full=Ste20-like serine/threonine protein kinase, putative {ECO:0000313|EMBL:EAL87038.1};
DE EC=2.7.11.1 {ECO:0000313|EMBL:EAL87038.1};
GN ORFNames=AFUA_7G04330 {ECO:0000313|EMBL:EAL87038.1};
OS Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 /
OS Af293) (Neosartorya fumigata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879 {ECO:0000313|EMBL:EAL87038.1, ECO:0000313|Proteomes:UP000002530};
RN [1] {ECO:0000313|EMBL:EAL87038.1, 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 -!- 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:EAL87038.1}.
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DR EMBL; AAHF01000009; EAL87038.1; -; Genomic_DNA.
DR RefSeq; XP_749076.1; XM_743983.1.
DR AlphaFoldDB; Q4WGA3; -.
DR STRING; 330879.Q4WGA3; -.
DR EnsemblFungi; EAL87038; EAL87038; AFUA_7G04330.
DR GeneID; 3506490; -.
DR KEGG; afm:AFUA_7G04330; -.
DR VEuPathDB; FungiDB:Afu7g04330; -.
DR eggNOG; KOG0201; Eukaryota.
DR HOGENOM; CLU_000288_2_1_1; -.
DR InParanoid; Q4WGA3; -.
DR OMA; FKEIERW; -.
DR OrthoDB; 152877at2759; -.
DR Proteomes; UP000002530; Chromosome 7.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd06609; STKc_MST3_like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR PANTHER; PTHR48012:SF10; SERINE_THREONINE-PROTEIN KINASE KIC1; 1.
DR PANTHER; PTHR48012; STERILE20-LIKE KINASE, ISOFORM B-RELATED; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:EAL87038.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000002530};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:EAL87038.1};
KW Transferase {ECO:0000313|EMBL:EAL87038.1}.
FT DOMAIN 11..261
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 287..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 659..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..316
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..349
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..364
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..395
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..498
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..548
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 688 AA; 76983 MW; A13B5F5483FD29C1 CRC64;
MEGMVDPETI YMRQNCIGGG SFGRVYKGVD KRTGNSVAIK VIDVENAEDE VEDIIQEIAI
LSELDSPYVT KYHGSFLKGS HLWIVMEFCS GGSCSDLLRP GPIPEDYIMI IMRELLRGLD
YLHTDKKLHR DVKAANILLT SNGQVKLADF GVSSQLSATM TKKNTFVGTP FWMAPEVIKQ
SGYDYKADIW SLGITAIELA QGEPPYSDIH PMKVLFLIPK NPPPTLQGPF SKTFKNFVEL
CLRRDPRERP SAKELLEHPF VKRARRTTYL TELIERYEGW QIRNGVQNGG VDEDCVQDLP
SNDKDREHEE DLWDFGTVRP VGRTTARGPM KEADTNTRNH NTTAWNFQDK SHEEVMKSSR
PQPDYPKKRS SFIATSASPT KVPLPPSPIK HPFSEVSPPR TPTRSQRPVA GQPTESPSTS
EYNRALQQSL AQDSVFLQLD LSPSSSSGPS KTGRVVPTAT AHATPYPSQD PTQISASRTE
RKPTVSEAQS QHHTHLPSHS RPPPTPSHIF PHPQQQTDTP RDRGSPEMSV RRFAPKNLSR
HIEETEPVPT KASEPQTVTP LLNVIVPALR TAVRRRREQV DLISRQAMAH SGENPDKLAE
IKGARQYVQV KIESLVDDLV HSFTRIDNWD NESPVGMGSG VVSFLEGFLE EILVRIEVPT
DDENDDEGYY PSKPADPDAR HTNNTSKT
//
