ID F9G1Z0_FUSOF Unreviewed; 862 AA.
AC F9G1Z0;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=FOXB_12672 {ECO:0000313|EMBL:EGU76775.1};
OS Fusarium oxysporum (strain Fo5176) (Fusarium vascular wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=660025 {ECO:0000313|EMBL:EGU76775.1};
RN [1] {ECO:0000313|EMBL:EGU76775.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fo5176 {ECO:0000313|EMBL:EGU76775.1};
RX PubMed=21942452; DOI=10.1094/mpmi-08-11-0212;
RA Thatcher L.F., Gardiner D.M., Kazan K., Manners J.;
RT "A highly conserved effector in Fusarium oxysporum is required for full
RT virulence on Arabidopsis.";
RL Mol. Plant Microbe Interact. 25:180-190(2012).
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:EGU76775.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AFQF01003174; EGU76775.1; -; Genomic_DNA.
DR AlphaFoldDB; F9G1Z0; -.
DR STRING; 660025.F9G1Z0; -.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR CDD; cd00180; PKc; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 3.
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; PTHR44329:SF214; ANKYRIN REPEAT-CONTAINING PROTEIN KINASE A-RELATED; 1.
DR PANTHER; PTHR44329; SERINE/THREONINE-PROTEIN KINASE TNNI3K-RELATED; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00248; ANK; 5.
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; 2.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 70..387
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REPEAT 572..604
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 802..834
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
SQ SEQUENCE 862 AA; 95028 MW; 63624BF93F7D5ED0 CRC64;
MSSGFQYNSS FTFSHPGWES DPVADYAELA LARVTAEAPD PGPIEDLTTF AQQLHTTGLP
ICEAADLEDL NDGAAIGSGT TMTVFKCLWK SKNKAVAVKR VNLGIALGHS QHEAHSQKYS
GLLKSLLREM RVMNHPWCKA HPNFVELLGI SWDAVTSDGG ISSYRPAMIV ELADPTMPQL
RDLVKSSRYP LDLKDQRMMF DLLADVAEGV TMLHAMKIVH GDLKPDNILL FRTKDRLVAK
LSDFGFCSPF TDIEYKIGGT PYWNAPKSFG LTKTDILAFQ ECMPDAPEEL RAFRKTITRD
LYSFGLVMAY SLFSILPYDE EGEHDADTTT VQDWKLHQDA SIFLHEQIIV YVLDFHSTNS
TRSGTSIETT SPVFRPKMVS SMGHGLQKRQ FGKSGFGCPP SAAKAREYET LAAQAGSDAA
QIQATFHGLV DGFDCSVTSE QKRVWLKTAI CIIFFGHNPD NARRNAFLDA LERVPVELLD
HAILYSFSKS FMDERIIYNL EFDGAAEDEL FSMVVNDERD KLVAALKSDM KLLGQKKGGF
TILHVAADYC REEIIQDLVR DFSMHPDTKS DYGDTPIERA AETGSIDCVR LLISLGADIK
PLADQELFSS VVITGTRNTI KDSPVSGTAS LLSLLCRAVE EDSEDPTSGQ TLINGRYMSG
NENEGIAPGS PLELAVSVLN YDSVIALLNL GADPNTYNYL PPLQIAVSLR EPLLALLLLT
HGALPNTVSR TDGDTALHCA NEVNGTEFAE APRNEIIPWQ QFVKEEVEAI DVDSDESLTA
RVKACITILL YFGADLEARN SEGETALVLA VRMGDYSTAK YLLQMGADIE SRDDEGNIAL
LGIESEQVQQ WCRDKELGIE TQ
//