GenomeNet

Database: UniProt
Entry: G0VKN0_NAUCC
LinkDB: G0VKN0_NAUCC
Original site: G0VKN0_NAUCC 
ID   G0VKN0_NAUCC            Unreviewed;       566 AA.
AC   G0VKN0;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   13-SEP-2023, entry version 55.
DE   RecName: Full=BRCT domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   Name=NCAS0J00880 {ECO:0000313|EMBL:CCC72067.1};
GN   OrderedLocusNames=NCAS_0J00880 {ECO:0000313|EMBL:CCC72067.1};
OS   Naumovozyma castellii (strain ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC
OS   1992 / NRRL Y-12630) (Yeast) (Saccharomyces castellii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX   NCBI_TaxID=1064592 {ECO:0000313|EMBL:CCC72067.1, ECO:0000313|Proteomes:UP000001640};
RN   [1] {ECO:0000313|EMBL:CCC72067.1, ECO:0000313|Proteomes:UP000001640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC 1992 / NRRL Y-12630
RC   {ECO:0000313|Proteomes:UP000001640};
RX   PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA   Wolfe K.H.;
RT   "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT   accidents.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Type strain:CBS 4309;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA   Wolfe K.H.;
RT   "Genome sequence of Naumovozyma castellii.";
RL   Submitted (AUG-2011) 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; HE576761; CCC72067.1; -; Genomic_DNA.
DR   RefSeq; XP_003678406.1; XM_003678358.1.
DR   AlphaFoldDB; G0VKN0; -.
DR   STRING; 1064592.G0VKN0; -.
DR   GeneID; 11525701; -.
DR   KEGG; ncs:NCAS_0J00880; -.
DR   eggNOG; KOG1181; Eukaryota.
DR   HOGENOM; CLU_019904_3_2_1; -.
DR   InParanoid; G0VKN0; -.
DR   OMA; TPYEFQL; -.
DR   OrthoDB; 69173at2759; -.
DR   Proteomes; UP000001640; Chromosome 10.
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; 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   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:UP000001640}.
FT   DOMAIN          79..172
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          166..263
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   REGION          272..566
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        302..344
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        374..404
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        405..427
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        441..515
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        516..539
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        547..566
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   566 AA;  63290 MW;  098596AB3A99B58E CRC64;
     MSSIDVVLTV GKLDASLALL TTQDHHVIEF PTMLLPENVK AGSIIKMGVS QDSDEELKQR
     DEFQSLQDQI LEKYGLEKPI APVLKVVNVT QTSCVLAWDK LSLGSAKLKA LTLYRHEERS
     MVVPNAFKIT QTKISGLSVD TDYEFQLKLS TTSGQFWSNK IKIHTHKMTD MSGITVCLGP
     LDPLQHITKE QISECLKEIH ARDLQTKVGI DTTHFVCNEL DDNGEEDEEL QKAKNNNIPI
     VKPEWIRACC VEKRIVGVRA FYVGAESTVS DDYKFPPLKN LPHPTQEQES PVEPVHEEVG
     SVPQETGTNE YESVPADNED TPQPSAMNEL NNDSESTFGK SVEPEVQESN IVEEQPPALG
     EEPEVQEPTT TETQEPALEK EPEVQGTQAE DVLPKEEELA TEPTKLEGTS ETQHIPESSV
     EQNEEEPQIV TENLEEDNTE DVEIIQPRID ISKEETLGSQ DELNTKSDDQ PNENTEQIED
     ASQPHELDST TTDKDTVTES LSEEVKEKVE DQGEPEQQPS IEEEGDNEED AEEEEEESES
     TPTPSKKKTT NKKKNNKKKG KKGKKK
//
DBGET integrated database retrieval system