ID A0A317WAV8_9EURO Unreviewed; 450 AA.
AC A0A317WAV8;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Chitin biosynthesis protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=BO70DRAFT_379283 {ECO:0000313|EMBL:PWY83483.1};
OS Aspergillus heteromorphus CBS 117.55.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448321 {ECO:0000313|EMBL:PWY83483.1, ECO:0000313|Proteomes:UP000247233};
RN [1] {ECO:0000313|EMBL:PWY83483.1, ECO:0000313|Proteomes:UP000247233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 117.55 {ECO:0000313|EMBL:PWY83483.1,
RC ECO:0000313|Proteomes:UP000247233};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PWY83483.1}.
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DR EMBL; MSFL01000010; PWY83483.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317WAV8; -.
DR STRING; 1448321.A0A317WAV8; -.
DR VEuPathDB; FungiDB:BO70DRAFT_379283; -.
DR OrthoDB; 69173at2759; -.
DR Proteomes; UP000247233; 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 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:UP000247233}.
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..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..404
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..424
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..444
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 450 AA; 49022 MW; EA684697D713CF59 CRC64;
MLVSLTVGKV DAGVAVLLTQ DNRLIEFPSV LLPNNITSGS IVDITVARNH VAETSSAASF
QTLQKRILNT YGIKTPTPPI LRLRNATQTS LVLEWDPIDL ATASLKSLSL YRNGSKAGSI
PRPLETRSTK ISGLAIHTEY TFHLVLRTTA GTYQSEKLTC RTHKMTDLSG ITVTAGVLPP
QQKDALATAL DRIGGKLIDT VRIDTTHFVC TEGRGPLWEK AVEMNIPVVV PEWVDACEAE
GTIVSVRGYY LNADPKARHL GPITSSTQHQ RTVSTATSNT LAPSQNQLQT PSRQSPQDGD
QPVEPPVTPF PGAEMTGQPI AEEKEVSSDE GEGDELPPPP PPPKDEDDNE EEEKENMEAG
EQNGEHETPP PPPQKDADAD AEENSSPAQS DQNEDEHEAA KAKEQEEEEE EEEEEEQEEV
EEEEDSSSSK AKERKSKEGG EEGDFNEVPL
//
