ID W6Z9S7_COCMI Unreviewed; 410 AA.
AC W6Z9S7;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Chitin biosynthesis protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=COCMIDRAFT_87077 {ECO:0000313|EMBL:EUC48502.1};
OS Bipolaris oryzae ATCC 44560.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=930090 {ECO:0000313|EMBL:EUC48502.1};
RN [1] {ECO:0000313|EMBL:EUC48502.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 44560 {ECO:0000313|EMBL:EUC48502.1};
RX PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT "Comparative genome structure, secondary metabolite, and effector coding
RT capacity across Cochliobolus pathogens.";
RL PLoS Genet. 9:E1003233-E1003233(2013).
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DR EMBL; KI963940; EUC48502.1; -; Genomic_DNA.
DR RefSeq; XP_007684954.1; XM_007686764.1.
DR AlphaFoldDB; W6Z9S7; -.
DR STRING; 930090.W6Z9S7; -.
DR GeneID; 19126981; -.
DR KEGG; bor:COCMIDRAFT_87077; -.
DR eggNOG; ENOG502QRF7; Eukaryota.
DR HOGENOM; CLU_019904_0_1_1; -.
DR OrthoDB; 69173at2759; -.
DR Proteomes; UP000054032; Unassembled WGS sequence.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR CDD; cd17742; BRCT_CHS5_like; 1.
DR CDD; cd13945; Chs5_N; 1.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 6.20.120.50; -; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR031673; Chs5_N.
DR InterPro; IPR031669; Fn3_2.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR47351; CHITIN BIOSYNTHESIS PROTEIN CHS5; 1.
DR PANTHER; PTHR47351:SF1; CHITIN BIOSYNTHESIS PROTEIN CHS5; 1.
DR Pfam; PF16892; CHS5_N; 1.
DR Pfam; PF16893; fn3_2; 1.
DR Pfam; PF12738; PTCB-BRCT; 1.
DR SMART; SM00292; BRCT; 1.
DR SMART; SM00060; FN3; 1.
DR SUPFAM; SSF52113; BRCT domain; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS50853; FN3; 1.
PE 4: Predicted;
FT DOMAIN 75..169
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 163..251
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 260..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..368
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 410 AA; 45058 MW; 228D4C781A629D3E CRC64;
MLVSLTVGKV DAGVAVLLTE DKRLIEFPSI LLPPDISSGS MVDIDVGRNY KAEADAQKAF
HELQSEIFRT FGQRTPSAPV LKCRNATQTS VVLEWDPIDI ATAELRSLTL YRNGNKAGTI
PKPTDQHSTK LSGLAVDTEY QFHLVLKTSA GTFSSEKLKV QTHKMTDLSG ITITPGHMPA
ALRESLQRSV ERIGAKIADT VRIDTTHFIC TDGRGPAWEK AVENNIPVVV PDWVIGCERE
GRIVGVRGYY LNADPRLRSV GAGSSQQQSQ QSSQPQQQQQ QQPQQQQQQQ QQQQQQPRSP
IISPRTEITP PTPEQSRQGR DAEGAAPPPP PKDDVSERSE RSSLESKSQT EDLKPQSGRE
KQQSGSEADD SEPEPSDEKS IEASLPQRVK PGQASVEEDD NGESFQDVQL
//
