GenomeNet

Database: UniProt
Entry: A0A2H1A5Q7_CANAR
LinkDB: A0A2H1A5Q7_CANAR
Original site: A0A2H1A5Q7_CANAR 
ID   A0A2H1A5Q7_CANAR        Unreviewed;       534 AA.
AC   A0A2H1A5Q7;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=BRCT domain-containing protein {ECO:0000259|PROSITE:PS50172};
GN   ORFNames=B9J08_000868 {ECO:0000313|EMBL:PIS58371.1}, CA7LBN_002420
GN   {ECO:0000313|EMBL:QWW23619.1};
OS   Candida auris (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis;
OC   Candida/Metschnikowiaceae.
OX   NCBI_TaxID=498019 {ECO:0000313|EMBL:PIS58371.1, ECO:0000313|Proteomes:UP000230249};
RN   [1] {ECO:0000313|EMBL:PIS58371.1, ECO:0000313|Proteomes:UP000230249}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B8441 {ECO:0000313|EMBL:PIS58371.1,
RC   ECO:0000313|Proteomes:UP000230249};
RX   PubMed=27988485; DOI=.1093/cid/ciw691;
RA   Lockhart S.R., Etienne K.A., Vallabhaneni S., Farooqi J., Chowdhary A.,
RA   Govender N.P., Colombo A.L., Calvo B., Cuomo C.A., Desjardins C.A.,
RA   Berkow E.L., Castanheira M., Magobo R.E., Jabeen K., Asghar R.J.,
RA   Meis J.F., Jackson B., Chiller T., Litvintseva A.P.;
RT   "Simultaneous emergence of multidrug-resistant Candida auris on 3
RT   continents confirmed by whole-genome sequencing and epidemiological
RT   analyses.";
RL   Clin. Infect. Dis. 64:134-140(2017).
RN   [2] {ECO:0000313|EMBL:PIS58371.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=B8441 {ECO:0000313|EMBL:PIS58371.1};
RA   Munoz J.F., Gade L.G., Chow N.A., Litvintseva A.P., Loparev V.N.,
RA   Cuomo C.A.;
RT   "Candida auris genome assembly and annotation.";
RL   Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:QWW23619.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CA7LBN {ECO:0000313|EMBL:QWW23619.1};
RA   Finianos M.;
RT   "Candida auris outbreak in lebanese hospital.";
RL   Submitted (JUN-2021) to the EMBL/GenBank/DDBJ databases.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; PEKT02000002; PIS58371.1; -; Genomic_DNA.
DR   EMBL; CP076750; QWW23619.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2H1A5Q7; -.
DR   STRING; 498019.A0A2H1A5Q7; -.
DR   EnsemblFungi; B9J08_000868-t37_1; B9J08_000868-t37_1-p1; B9J08_000868.
DR   VEuPathDB; FungiDB:B9J08_000868; -.
DR   VEuPathDB; FungiDB:CJI96_0003230; -.
DR   VEuPathDB; FungiDB:CJI97_000886; -.
DR   VEuPathDB; FungiDB:CJJ07_004456; -.
DR   VEuPathDB; FungiDB:CJJ09_002829; -.
DR   VEuPathDB; FungiDB:QG37_02809; -.
DR   OMA; EFWDLQR; -.
DR   OrthoDB; 69173at2759; -.
DR   Proteomes; UP000230249; Unassembled WGS sequence.
DR   Proteomes; UP000825438; Chromosome II.
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; 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.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000230249}.
FT   DOMAIN          164..259
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   REGION          276..534
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        292..306
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        307..324
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        326..340
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        341..383
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        403..449
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        464..485
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        486..507
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   534 AA;  58850 MW;  50EE28850EA24ECC CRC64;
     MVEVSLTVGK LDASLALLLT KDHHLIEFPT ILLPNGVKAG SIVKIRCDRD LETELEEKKQ
     FQAIQDEIIN TFGKNLPKAP QLRVKNVTQT SCVLEWDQLD LGTASLKNLV LFRDGKKLGA
     IPQAMTNKTT KLSGLPIDKT FKFHLRLDTT AGVYKSEEVE VTTHKMTDLS GITVCLGDIT
     PNDQFTVEDI QAALKNMGAH HPAQETVKVD TTHFITMREN KQNPEYVKAN DMNIPIIRPE
     WLKACERERR IVGVRDFYVK DCSLPDILAR NYWKKDAPAK STEASKDTLE GPPVVQVTSP
     SPETTSKQDL NEKDEGKDSG VPSSEAVEEA KSSENTSGEV SESSKKSEKE GEVKSDEKPD
     ENATVDVTKN EDEVGRTDEL DNAQKASETS MSLREEESTK QAIAEPTEQV VTDSKEKTNT
     NAVEGTPNAA SIETQQAETS AQPTAEELTE VDLNESHPES GVAESTDLPK KIEKEEIQEA
     KEDDTIAEGV DGDEGDENDD DDENENANGK ETTDQPAGES KSKKKNKKKK KGKK
//
DBGET integrated database retrieval system