ID F0XRG4_GROCL Unreviewed; 1439 AA.
AC F0XRG4;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE SubName: Full=Ankyrin repeat-containing protein {ECO:0000313|EMBL:EFW99917.1};
GN ORFNames=CMQ_235 {ECO:0000313|EMBL:EFW99917.1};
OS Grosmannia clavigera (strain kw1407 / UAMH 11150) (Blue stain fungus)
OS (Graphiocladiella clavigera).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Grosmannia.
OX NCBI_TaxID=655863 {ECO:0000313|Proteomes:UP000007796};
RN [1] {ECO:0000313|EMBL:EFW99917.1, ECO:0000313|Proteomes:UP000007796}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=kw1407 / UAMH 11150 {ECO:0000313|Proteomes:UP000007796};
RX PubMed=21262841; DOI=10.1073/pnas.1011289108;
RA DiGuistini S., Wang Y., Liao N.Y., Taylor G., Tanguay P., Feau N.,
RA Henrissat B., Chan S.K., Hesse-Orce U., Alamouti S.M., Tsui C.K.M.,
RA Docking R.T., Levasseur A., Haridas S., Robertson G., Birol I., Holt R.A.,
RA Marra M.A., Hamelin R.C., Hirst M., Jones S.J.M., Bohlmann J., Breuil C.;
RT "Genome and transcriptome analyses of the mountain pine beetle-fungal
RT symbiont Grosmannia clavigera, a lodgepole pine pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:2504-2509(2011).
CC -!- SIMILARITY: Belongs to the putative lipase ROG1 family.
CC {ECO:0000256|ARBA:ARBA00007920}.
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DR EMBL; GL629807; EFW99917.1; -; Genomic_DNA.
DR RefSeq; XP_014169332.1; XM_014313857.1.
DR STRING; 655863.F0XRG4; -.
DR GeneID; 25975329; -.
DR eggNOG; KOG2029; Eukaryota.
DR eggNOG; KOG4177; Eukaryota.
DR HOGENOM; CLU_000288_34_1_1; -.
DR InParanoid; F0XRG4; -.
DR OrthoDB; 1951763at2759; -.
DR Proteomes; UP000007796; Unassembled WGS sequence.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 6.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR007751; DUF676_lipase-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR24171; ANKYRIN REPEAT DOMAIN-CONTAINING PROTEIN 39-RELATED; 1.
DR PANTHER; PTHR24171:SF8; BRCA1-ASSOCIATED RING DOMAIN PROTEIN 1; 1.
DR Pfam; PF00023; Ank; 3.
DR Pfam; PF12796; Ank_2; 5.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF05057; DUF676; 1.
DR SMART; SM00248; ANK; 18.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 14.
DR PROSITE; PS50088; ANK_REPEAT; 15.
PE 3: Inferred from homology;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Reference proteome {ECO:0000313|Proteomes:UP000007796}.
FT DOMAIN 172..279
FT /note="DUF676"
FT /evidence="ECO:0000259|Pfam:PF05057"
FT REPEAT 836..860
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 870..894
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 904..928
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 938..962
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 972..996
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1006..1030
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1040..1064
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1074..1098
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1108..1132
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1142..1166
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1176..1200
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1210..1242
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1243..1275
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1345..1378
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1413..1433
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1439 AA; 159049 MW; F39FB605897D1FDB CRC64;
MADNNDQEFS STSSAVAVSN AMAKAGEPSS VAETFPFAPR RQKLKQKAMR LFRPRNMPPK
AKAVANTIVY TDQQRAGPSK IPNPPEESSV PVPFPDGIKV LHDCSDARVD VCFIHGLSGD
REKTWTAAGE SQPWSQTLLP SRLPGARILT YGYDAYVVRV TSAANNSLTN HATNLLKDLT
DDRAASRASS RPIIFVAHSL GGIVCKKALL LSRNNRDAHL QSIFKWTKGV AFMGTPHRGS
EVADWAMLPA SALGFMKTVN KTLLEVLRTD DVMLKDTREQ FVAMIQDLVL NGRIVEIACF
CEELPMSNLK KFIVTQDSAT LEGYNAFTIH ADHRGMVRFR SEDDNGFKRL LGDLVRWTLP
QEPVVEIPLQ PVLSELDKDC LSSLAFPKMN DRMNDIESAF DNTCNWLFQH ETYSSWEATD
RGLLWIKGKP GSGKSTLLRH SLNRTNKLPP CGSQPPLILS FFFHGRGEEL QKSPLGLFRA
LLHQILSQAP DAAKDLVATF QDRRNTMGSA GGQWKWHARE LRDHFQASLP QVIESRTVWI
FVDALDECGE QNAVELAGHF QRILYQLPPT AGQCRICFTC RHYPILSLDP ATFEICVEQE
NGLDIETYVY NKFSSFNVPA EIVATITSQA SGVFMWTYLV LNTVRDLLRG GAGWKKIASK
ISETPQDLDT LYDELVKSMD DTEASLKLFQ WICFARRPLS LDELRWALIL DPGCSYTSVQ
QCKSADEYEC DMEKHLKTLS RGLAELTQSS DEPVVQFIHQ SVQDFFVNKG LLSLHNKKSD
AAETVTVILQ DTSADVNATD GIGRTPLSYA AYAGNESTVH QILKIGKVDV DSEDQYGWTP
LFLAARYGHQ TVVKQLLDTG KVDVDSKDRD GRTPLSWAAE NGHQTVVKQL LDTGKVDVDL
KDHYGRTPLS WAAKKGHQTV VKQLLDTGKV DVDLKDRDGR TPLSRAARYG HQTVVKQLLD
TGKVDVDLKD HYGRTPLSWA ARYGHQTVVK QLLDTGKVDV DSKDRDGRTP LSWAAENGHQ
TVVKQLLDTG KVDVDLKDRD GRTPLSWAAE NGHQTVVKQL LDTGKVDVDS KDRDGRTPLS
WAAENGHQTV VKQLLDTGKV DVDLKDRDGR TPLSWAAEKG HQTVVKQLLD TGKVDVDSKD
RDGRTPLSWA ARYGHQTVVK QLLDTGKVDV DSKDQGGWTP LSWAAENGHQ TVVKQLLDTG
KVDVDSKDQG GWTPLSWAAE NGHQTVLSLL MQSGGDAKRG DNVGRSLLLI AAENGDEPTV
QLLLSATTSL DSKSSQTGTL PMTLQQVVQG ELEAMVSFLS QVDAKSGVDD RRYETALVWA
SKAGYTDVVQ LLLTMDGIDV NHKIDGETAL LQSAKNGRVE VVKRLLAADG IDVNRKSWKE
QTALMRSAEE GHTSVVTLLL TVDGIDIACK SRYGMTALDL AAKGGHLDVV ELLEQKLHG
//