ID F0XKZ5_GROCL Unreviewed; 1339 AA.
AC F0XKZ5;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Aminotransferase class 3 {ECO:0000313|EMBL:EFX01809.1};
GN ORFNames=CMQ_8275 {ECO:0000313|EMBL:EFX01809.1};
OS Grosmannia clavigera (strain kw1407 / UAMH 11150) (Blue stain fungus)
OS (Graphiocladiella clavigera).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Leptographium.
OX NCBI_TaxID=655863 {ECO:0000313|Proteomes:UP000007796};
RN [1] {ECO:0000313|EMBL:EFX01809.1, 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).
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DR EMBL; GL629788; EFX01809.1; -; Genomic_DNA.
DR RefSeq; XP_014171291.1; XM_014315816.1.
DR STRING; 655863.F0XKZ5; -.
DR GeneID; 25981912; -.
DR eggNOG; ENOG502RK0Z; Eukaryota.
DR HOGENOM; CLU_258489_0_0_1; -.
DR InParanoid; F0XKZ5; -.
DR OrthoDB; 1537817at2759; -.
DR Proteomes; UP000007796; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 4: Predicted;
KW Aminotransferase {ECO:0000313|EMBL:EFX01809.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000007796};
KW Transferase {ECO:0000313|EMBL:EFX01809.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 16..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 978..1284
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 130..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 415..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 536..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 619..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 657..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 783..969
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1309..1339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..442
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..487
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..685
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 783..800
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 801..818
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 844..858
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 869..967
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1339 AA; 142250 MW; 4A6470B5092DF4E9 CRC64;
MSSTAAGGGG GSSLSIGVIV AIAVVGTVVM AVAAGVLCAY LAHQRRLRLN ARQMQQTTAR
QSSQVAVQQG GLPIGDHSTK AAARQYFNTR SVAAGASSAD SWSVEADSAF EGTGFTWWWR
CRWRRWQRQQ GRQDRQGGPE HGADGELPLF GSGDSSRVKQ PRTRNKLQRP RPAAPKMVSS
SNFAFVPVPV EMPARSKRSS NDGSGGDAGK DGVSPSKQMR PQRPPPPPPQ LRLITHDLGS
QIDTSDAGAG AVPHPANVLV ATQSQQELQQ GYQNYQNYQN YQNYQNYQNY QNYQNYQNFE
HHQNTKNGRQ FAGTPYAYAE KRLQQLQAQA QTEQPASTAG YTGDDDDDVF AAVPTLARQR
QQCLAEEAAA REAAAAASAM AMTVEEALVV PEAQKSQRSS QESGVSEADS MFVEEATTTA
LSSPSRSPTR TTDQSSTISV AAKPPTMHLV PRADTAELVK TAEHEAADAS TSPDSGSSSA
YSPLSTRSSL STVYSADERP EAAKKAAGLG ITMNRRSVLM QLPVWQQQQQ YLKQQQQQKQ
KEQKQQKQKQ KPQGVQINNG IRGSFGGAVA PILVAPAAVR ARSASSASVT APLLLQPSRS
SNPAAPSSAI RVLVTSPTAN SLTGSSSSSP GKRGNVTLDV TDRTDTAHVQ IGENASATAA
AEEEIRRQQQ QQQQQQQRRQ SLVPPPTNLA SLVEVLADVP ENGEAVGAGR RWSTRPLPVA
PSRLSAASLK QQQQQEVETD NRASTLTTNS LLATAVELRR MNSVAHSEAS TVYSEATNIS
PLPPQMAVFP GSSTTADTKD EKATTPLRRG RRSRVLEGTA ASKRGSRASG TGSRHYLSLG
GAAGSGTNAG SSSSDKENGT EESVVEGGPA VSMQTTSGSK RQQPRPFSIV AGQESAELAS
LSTPRRTPSR SPSKTDRSTS SCVVVSSNSA VKTPGSRSPT KNKSARRTSA SQGTPTRTPT
QSSPPTAAMA PLPIAGGPKV VLYHQTHHTP TGEPVSVLPL LRRDGDMGPS VTHVIVGAIH
LNADPAAPTL NDHHPDDSRF DMLWAEVGAL QQAGVRVLGM LGGAAKGSYA RLDVGLLEGH
SAASATSASF EAYYAALHRL VRRQRLDGID LDVEEPMSLA GIVHLIDRLR RDFGPGFLIT
MAPVAASLLR PTEPRCNLSG FSYADVEQRR GRDVAWYHAQ FYCGWGDASS PDIYLAMTRG
AVAPISGLGP HRVVMGLLTN PANGPGWVDL DISTTVLLDL CAAAQTDASY FAGVSGWEYF
NALPGAQARP WEWAEWMSAI LGSSVEAANG FGIQGVAAAA AAAITETAHT TEADPDGEAG
LEAPVPDPFE YDYQSDTEE
//
