ID A0A2B7ZM76_9EURO Unreviewed; 426 AA.
AC A0A2B7ZM76;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Chitin biosynthesis protein CHS5 {ECO:0008006|Google:ProtNLM};
GN ORFNames=GX50_03075 {ECO:0000313|EMBL:PGH34112.1};
OS Emmonsia crescens.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emmonsia.
OX NCBI_TaxID=73230 {ECO:0000313|EMBL:PGH34112.1, ECO:0000313|Proteomes:UP000226031};
RN [1] {ECO:0000313|EMBL:PGH34112.1, ECO:0000313|Proteomes:UP000226031}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH4076 {ECO:0000313|EMBL:PGH34112.1,
RC ECO:0000313|Proteomes:UP000226031};
RA Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL Submitted (OCT-2017) 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:PGH34112.1}.
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DR EMBL; PDND01000047; PGH34112.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B7ZM76; -.
DR STRING; 73230.A0A2B7ZM76; -.
DR VEuPathDB; FungiDB:EMCG_02140; -.
DR OrthoDB; 69173at2759; -.
DR Proteomes; UP000226031; 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;
KW Reference proteome {ECO:0000313|Proteomes:UP000226031}.
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 261..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..379
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 426 AA; 45639 MW; FCC3A55EBC368383 CRC64;
MLVSLTVGKV DAGVAVLLTQ DNRLIEFPSV LLPKNIGSGS IVDITVSRNQ AAEAASIAAF
QSLQKRILHT YGIHTPSAPV LRLRNATQTS LVLEWDPINL ATASLKSLSL YRNDSKAGSI
PRPKEMLSTK ISGLAIDTEY TFHLVLRTSA GTFSSEKLVC RTHKMTDLSG ITVTPGVLPP
SLKASLEETV DRIGAKLIDT VRIDTTHFVC TEGRGAAWEK AVEMNIPVVR PEWVEGCERE
GTIVSVRGYY LNADPKLRQI GPGVGAQQHR QQATLNNSSG SLSAGRMDRT NSTSRSPEQR
VEKELPSTPL PGSGVNGPSR ALKSENGDEN GDETQSAPQS LPKDGKENAK PSQEDVGSPV
DEDEIPPGYG DKEADYESDT ADSSNGDLVN KTNSQSQRRQ KSPVGTSSDK KTNGTGGEGE
LDEVPL
//
