ID G0S177_CHATD Unreviewed; 399 AA.
AC G0S177;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 13-SEP-2023, entry version 46.
DE RecName: Full=Chitin biosynthesis protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=CTHT_0012620 {ECO:0000313|EMBL:EGS22787.1};
OS Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
OS (Thermochaetoides thermophila).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermochaetoides.
OX NCBI_TaxID=759272 {ECO:0000313|Proteomes:UP000008066};
RN [1] {ECO:0000313|EMBL:EGS22787.1, ECO:0000313|Proteomes:UP000008066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1495 / CBS 144.50 / IMI 039719
RC {ECO:0000313|Proteomes:UP000008066};
RX PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA Arumugam M., Bork P., Hurt E.;
RT "Insight into structure and assembly of the nuclear pore complex by
RT utilizing the genome of a eukaryotic thermophile.";
RL Cell 146:277-289(2011).
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DR EMBL; GL988039; EGS22787.1; -; Genomic_DNA.
DR RefSeq; XP_006691779.1; XM_006691716.1.
DR AlphaFoldDB; G0S177; -.
DR STRING; 759272.G0S177; -.
DR GeneID; 18255300; -.
DR KEGG; cthr:CTHT_0012620; -.
DR eggNOG; ENOG502QRF7; Eukaryota.
DR HOGENOM; CLU_019904_0_0_1; -.
DR OMA; HKMTDLR; -.
DR OrthoDB; 69173at2759; -.
DR Proteomes; UP000008066; Unassembled WGS sequence.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
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:UP000008066}.
FT DOMAIN 76..170
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 164..252
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 265..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..335
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..390
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 399 AA; 43339 MW; 00F34574063634EE CRC64;
MGVVSLTVGK VDAGVTVLLT PDKRLIEFPS ILLPPDIRSG SIVDINVSRN KSSEAAAERA
FRDLQDQILS SFGTHSPSPP TLRVRNTTQT SVVLEWDPLQ LATADLISLS LYRNGQKAGT
IPKPLTMHTT KISGLAVDTE YTFHLVLRTT AGTYASPRIT VRTHKMTDLS GITITTGILP
SHVRENLLAV VERIGAKVVD GVRIDTTHFV TTEGRGVQWE KANELNIPVV RPEWVEACER
AGRILGVTKF YLDAARVGAL FDERPGTAGT VGSGSAPPPP PPPKEQKVQS PVQTRTEVTV
EKPKEESPEP ASGSEKEQQQ QKEEGEKKAD EQSSQSAEEK PLPSRPKVTV EDEKEEEEKE
EEKEKEKAKA PAAEEKEGSS GDEKDGKSPG DSSFQDVAL
//
