ID Q2UHL7_ASPOR Unreviewed; 974 AA.
AC Q2UHL7;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=AO090023000397 {ECO:0000313|EMBL:BAE58948.1};
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516 {ECO:0000313|EMBL:BAE58948.1, ECO:0000313|Proteomes:UP000006564};
RN [1] {ECO:0000313|EMBL:BAE58948.1, ECO:0000313|Proteomes:UP000006564}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40 {ECO:0000313|Proteomes:UP000006564};
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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DR EMBL; AP007157; BAE58948.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2UHL7; -.
DR EnsemblFungi; BAE58948; BAE58948; AO090023000397.
DR VEuPathDB; FungiDB:AO090023000397; -.
DR HOGENOM; CLU_012876_0_0_1; -.
DR OMA; YTFCPID; -.
DR OrthoDB; 2143541at2759; -.
DR Proteomes; UP000006564; Chromosome 3.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24161; ANK_REP_REGION DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR24161:SF85; LD20463P-RELATED; 1.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00248; ANK; 4.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50297; ANK_REP_REGION; 3.
DR PROSITE; PS50088; ANK_REPEAT; 3.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000006564};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00023315};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 911..933
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 940..957
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 298..628
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REPEAT 727..759
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 760..786
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 865..891
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 38..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 974 AA; 109619 MW; 4CD0D0AED0E5A90C CRC64;
MSRYDDFRIA FNVEMSNEEI DAALTANGLI ALHHALSSSS GYHSNDSSHR PSSEAHRRFT
RRLTPTEHTT PRTIPNLRQS PELEMNEISP RQTYFHNDRP YYDVYPGPTN TIHRAENIIG
ESHLYPHDPL FIESPPERRP SIQRELMLRE LSLALQTETH RRDRPSEKVV TRHSLALIWS
ESRLERFIDL VRPGFDNTWM HNIREEWLQT LSILVDIGWQ DWGRFGDIFL KHRDEHGKWD
RSDRMIPTYT LAILEDDSFL GSPWAEKFQA SQYTFCPIDI EEGKSLTFSK EWKLPFVNDI
STSIGNGAYG RVTKEIIGSG HFRSQSEHHL PGAPYSKDIA VALKQFEGRG DFHSETNNLD
VLRSSLSKHD RIVPFLATVT IGNSFNILSP LADMDLDVFL REGHQRCPDF TLRDLMQEAA
HLAGALAFLH QGLDSNPPGL SCCHMDLKPG NILVFHGDAL DFPKVGKWKI SDFGISIMSR
PERTGTTVTE FVDSFTQRQR LSPPPGPYQS PDGAGHGLKS DIWSLGCILT RILALGLEGA
DGMMHLDQLR GTDGDGASPY ENDYFHRGSP PVLNPHVQSW LSGLTSGRYN YNQEFLTRCQ
SLIVSMLAIS HDDRPSARNV QEELHNLVEI AQPIVLRTPS INTSVGGSAS VGSGSDNIRV
NSRDIQPGNE RLLSEVINLW NGDVNIEGIW DGNDRLLIYL IRLDYATALE VLLARHPGLD
LETPDSKGDT PLKIAAAAGK RHIVEMLLNA GANIDAPSRR GGTPLMPACR HGHVSTVRLL
LDRGADCSSH CEDGYTCLHY AIYSDNGANI IQLLNGKVSF NIRRSRTDET PLLSLIVRYD
GTESWWDKFG RLLQGSADIN MADIHRFTPL SRAVEQGHSQ LAAILLSQGA NYRDNPFVPV
PVPVSVFSLY LFHYFSVLII AFLLLLLLLL LLLLLRLIRL FLVSLGVSFF FLFLYLGKMV
RFCCEEKRVA CIKE
//
