ID G2WW04_VERDV Unreviewed; 418 AA.
AC G2WW04;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 03-MAY-2023, entry version 48.
DE SubName: Full=Chitin biosynthesis protein CHS5 {ECO:0000313|EMBL:EGY19774.1};
GN ORFNames=VDAG_01790 {ECO:0000313|EMBL:EGY19774.1};
OS Verticillium dahliae (strain VdLs.17 / ATCC MYA-4575 / FGSC 10137)
OS (Verticillium wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=498257 {ECO:0000313|EMBL:EGY19774.1, ECO:0000313|Proteomes:UP000001611};
RN [1] {ECO:0000313|Proteomes:UP000001611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VdLs.17 / ATCC MYA-4575 / FGSC 10137
RC {ECO:0000313|Proteomes:UP000001611};
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; DS572697; EGY19774.1; -; Genomic_DNA.
DR RefSeq; XP_009656114.1; XM_009657819.1.
DR AlphaFoldDB; G2WW04; -.
DR STRING; 498257.G2WW04; -.
DR EnsemblFungi; EGY19774; EGY19774; VDAG_01790.
DR GeneID; 20703253; -.
DR KEGG; vda:VDAG_01790; -.
DR eggNOG; ENOG502QRF7; Eukaryota.
DR HOGENOM; CLU_019904_0_0_1; -.
DR InParanoid; G2WW04; -.
DR OMA; HKMTDLR; -.
DR OrthoDB; 69173at2759; -.
DR Proteomes; UP000001611; Chromosome 7.
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 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;
KW Reference proteome {ECO:0000313|Proteomes:UP000001611}.
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 253..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..336
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..373
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 418 AA; 44345 MW; EE92B3EE29430592 CRC64;
MLVSLTVGKV DAGVTVLLTP DKRLIEFPSI LLPPNISSGS IVDITVGRNN ASESAAEHAF
RDLQERIYDA FGASEPAVPV LRCRNATQTS VVLEWDPVEL ATADLLSLSL FRNGQKAGSI
PRPLHMHSTK ISGLAVDTDY TFHLVLRTTA GTFASDKVHV RTHKLTDLSG ITITPGVMPQ
QTRDALAAAV ERIGAKLVDG VRIDTTHFVT TEGRGPAWEK AVDTNIPVVR PEWVDACEKN
GRILGVTKFY LDAMRPGPPT PGIEEPSQKD LPAPPAQQQQ QQQQRVPPAA AAAAPEASAA
DDGPPAGYSA APAPTSGSAS GDEDEVEDED EEDQDEGKDS KSSPTEGAAT TEPKTRAAEQ
EEQKVRLEDK SEQNLALRPG GPSQGSLSAA ASEDGRGDED TPDQPGSSSR ASFQNVEL
//
