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Database: UniProt
Entry: C9SYH2_VERA1
LinkDB: C9SYH2_VERA1
Original site: C9SYH2_VERA1 
ID   C9SYH2_VERA1            Unreviewed;       820 AA.
AC   C9SYH2;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   SubName: Full=Ankyrin repeat and protein kinase domain-containing protein {ECO:0000313|EMBL:EEY23837.1};
GN   ORFNames=VDBG_09947 {ECO:0000313|EMBL:EEY23837.1};
OS   Verticillium alfalfae (strain VaMs.102 / ATCC MYA-4576 / FGSC 10136)
OS   (Verticillium wilt of alfalfa) (Verticillium albo-atrum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX   NCBI_TaxID=526221 {ECO:0000313|Proteomes:UP000008698};
RN   [1] {ECO:0000313|Proteomes:UP000008698}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VaMs.102 / ATCC MYA-4576 / FGSC 10136
RC   {ECO:0000313|Proteomes:UP000008698};
RX   PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA   Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA   Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA   Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., Santhanam P.,
RA   Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., Inderbitzin P.,
RA   Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., Galagan J.,
RA   Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT   "Comparative genomics yields insights into niche adaptation of plant
RT   vascular wilt pathogens.";
RL   PLoS Pathog. 7:E1002137-E1002137(2011).
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DR   EMBL; DS985230; EEY23837.1; -; Genomic_DNA.
DR   RefSeq; XP_002999907.1; XM_002999861.1.
DR   AlphaFoldDB; C9SYH2; -.
DR   STRING; 526221.C9SYH2; -.
DR   GeneID; 9531726; -.
DR   KEGG; val:VDBG_09947; -.
DR   eggNOG; KOG4177; Eukaryota.
DR   HOGENOM; CLU_009139_0_0_1; -.
DR   OMA; HTIISAY; -.
DR   OrthoDB; 2477520at2759; -.
DR   Proteomes; UP000008698; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 3.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   PANTHER; PTHR24161; ANK_REP_REGION DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR24161:SF85; LD20463P-RELATED; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF13637; Ank_4; 3.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 8.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 7.
DR   PROSITE; PS50088; ANK_REPEAT; 7.
PE   4: Predicted;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW   ProRule:PRU00023}; Kinase {ECO:0000313|EMBL:EEY23837.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008698};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000313|EMBL:EEY23837.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        692..719
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REPEAT          42..74
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          77..109
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          110..142
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          143..175
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          176..200
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          210..242
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          243..275
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          402..451
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          735..795
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        425..447
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        744..779
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   820 AA;  90487 MW;  9D8574C1C03481CC CRC64;
     MESQSPMLEE VISSQPDDKE TEEHVHQLLI SLPSVFFTID AQKRTPLHHA ASAGKSNILR
     AILTVGPESE VDLQDAEGCT ALHLAARNGH EAVARALLNV GADVRREEAF GETPLHEAAR
     NGHAALVKLF IDSGAVVDVG NRDSSTALHV AARRGHSDVV EILLTAGANP ATKDKVGDTP
     LHDAAREGRT DIVDALLNTG LVSVEARNAN GLTPLSVGAR HGRDGIVRSL LERGADVDAQ
     SSEFCTPLHQ AATEGHDGVA RSLIAAGAEV DLQDKDLQSP LHTAVIFEHA DVTRERLRSA
     MTGSRDVAPR RELLRASTAE RTRRLSAMPT GLQHHLFPYL KHLDAMNSLR QSFTKSELHV
     PRTLDQSYHE SLSKEEVRAR NESQVLYRYL LRLESLVKAE KQKNDGSIVA GEQKSGQGSG
     NPFEHRELLE QHSDKQKRTD GTKEQLMRMA GRQDVASSVR ARVARERKGI EQEQRKQVLM
     VSQLWMWRID EHNIITCYPE RWDDKNAKTL LNEIKHRVLA SPGLKSADTD MMDIAAHVLE
     SAVGFSEEEF HFQFCGPRSY CNVFAGSVAF LSNEAMKRYA AFKSSIRGMR TSKTVLGDLR
     AEIELLQEID DVREEVNMIQ TVLKEQERVV VEFQGSREPD CTVLEQVRGG LGGFSHPTLD
     FFDRLGLDAD RVRTSREANI EEALSANEQS KILFIFTGAT VVFKVGSLLA TVLVIWLSLQ
     IYELVAQGQS SAKRRKLDSM LRRKTQPTET LAPEATAQSQ RGDESAGPAS QTARSSALRS
     EAAASAVGQG ASGQRKLRKR FIRFGRDGKK RLDEETAIVV
//
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