ID A0A421JVL3_9ASCO Unreviewed; 524 AA.
AC A0A421JVL3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 22-FEB-2023, entry version 10.
DE SubName: Full=Chitin biosynthesis protein CHS5 {ECO:0000313|EMBL:RLV96080.1};
GN ORFNames=JA1_000521 {ECO:0000313|EMBL:RLV96080.1};
OS Spathaspora sp. JA1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Spathaspora.
OX NCBI_TaxID=2028339 {ECO:0000313|EMBL:RLV96080.1, ECO:0000313|Proteomes:UP000285775};
RN [1] {ECO:0000313|EMBL:RLV96080.1, ECO:0000313|Proteomes:UP000285775}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA1 {ECO:0000313|EMBL:RLV96080.1,
RC ECO:0000313|Proteomes:UP000285775};
RA Formighieri E.F., Steindorff A.S., Trichez D., Almeida J.R.;
RT "Physiological and comparative genomic analysis of newly identified yeasts
RT Spathaspora sp. JA1 and Meyerozyma sp. JA9 reveals insights into xylitol
RT production.";
RL Submitted (AUG-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:RLV96080.1}.
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DR EMBL; NSGQ01000003; RLV96080.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A421JVL3; -.
DR STRING; 2028339.A0A421JVL3; -.
DR Proteomes; UP000285775; 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 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; IPR013783; Ig-like_fold.
DR PANTHER; PTHR47351; CHITIN BIOSYNTHESIS PROTEIN CHS5; 1.
DR PANTHER; PTHR47351:SF1; CHITIN BIOSYNTHESIS PROTEIN CHS5; 1.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF16892; CHS5_N; 1.
DR Pfam; PF16893; fn3_2; 1.
DR SMART; SM00292; BRCT; 1.
DR SUPFAM; SSF52113; BRCT domain; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS50853; FN3; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000285775}.
FT DOMAIN 76..170
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 164..259
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 293..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..309
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..354
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..478
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..500
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 524 AA; 58738 MW; 7633EECB47D581C1 CRC64;
MVEVSLTIGK LDASLALLLT KDHHLIEFPT ILLPNGVKAG SIVKIKCDQD LISEQEEAAQ
FEQIQQEILS SFATNLPQVP KLRVKNVTQT SCVLEWDQLD LGTANLKNLI LFKDGKKLGS
IPSPSTNKTS KLSGLPIDKS FKFQLRLDTT AGTFLSDEIE VNTHKMTDLS GITVCLGDFS
ANDPFTRDDI EETLRTMGAK YPPQDQVKVD TTHFLCTREN KQNAEYIKAN EMNIPIIRPE
WLKACERERR IVGVRDFYVK DCVLPDIFAK NYWKNSKVEP AQELPEVVQE VAKEEVPAKE
EEKELPEAEP VPEQVPAAPE EVPEEAEAAA EPPQIEISHP ETEDKEETQK DIDDAFGEPT
SGGSLGEEIE QEEISHSTPE PVTIDEPQPV EPVEVVTEAY VEVVYDEDVL VEDPQETEIN
VEVEQNVAKE EPLEEVALDA AEPKVEATDA TEEKLEQVDL EETTETKVEI KEIPAEEAVE
TEEVPLDDDQ EDDDEEEDTK DPATSTTNSD QDKKKKRKKK NKKK
//
