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Database: UniProt
Entry: I2H6K4_TETBL
LinkDB: I2H6K4_TETBL
Original site: I2H6K4_TETBL 
ID   I2H6K4_TETBL            Unreviewed;       784 AA.
AC   I2H6K4;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   RecName: Full=BRCT domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   Name=TBLA0G00570 {ECO:0000313|EMBL:CCH62006.1};
GN   ORFNames=TBLA_0G00570 {ECO:0000313|EMBL:CCH62006.1};
OS   Tetrapisispora blattae (strain ATCC 34711 / CBS 6284 / DSM 70876 / NBRC
OS   10599 / NRRL Y-10934 / UCD 77-7) (Yeast) (Kluyveromyces blattae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX   NCBI_TaxID=1071380 {ECO:0000313|EMBL:CCH62006.1, ECO:0000313|Proteomes:UP000002866};
RN   [1] {ECO:0000313|EMBL:CCH62006.1, ECO:0000313|Proteomes:UP000002866}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 34711 / CBS 6284 / DSM 70876 / NBRC 10599 / NRRL Y-10934 /
RC   UCD 77-7 {ECO:0000313|Proteomes:UP000002866};
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).
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DR   EMBL; HE806322; CCH62006.1; -; Genomic_DNA.
DR   RefSeq; XP_004181525.1; XM_004181477.1.
DR   AlphaFoldDB; I2H6K4; -.
DR   STRING; 1071380.I2H6K4; -.
DR   GeneID; 14497138; -.
DR   KEGG; tbl:TBLA_0G00570; -.
DR   eggNOG; KOG1181; Eukaryota.
DR   HOGENOM; CLU_019904_3_0_1; -.
DR   InParanoid; I2H6K4; -.
DR   OMA; WIRACEV; -.
DR   OrthoDB; 69173at2759; -.
DR   Proteomes; UP000002866; Chromosome 7.
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:UP000002866}.
FT   DOMAIN          78..172
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          166..261
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   REGION          282..784
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        305..322
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        323..366
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        379..398
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        419..436
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        437..452
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        469..487
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        507..552
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        561..590
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        596..611
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        618..665
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        666..691
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        722..751
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        752..768
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        769..784
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   784 AA;  86827 MW;  727DA0614757CD6A CRC64;
     MSQIDVVMTV GKLDASLALL TTQDHHVIEF PTMLLPETVK AGSIVKMTVA QDTEEENKQR
     TSFKLLQNVI LEKYGTEKPK NPLLKIINIT QTSCVLQWDT ISLGSARFKS LILYKQGIRA
     MVIPNPFKVT STKISGLSVD KPYDFQLKLS TTSGDFWSEK VKVHTHKMTD MSGITVCLGP
     LDPLKKITRN QIATSLRKIG AKQLQDHVSI DTTHFITNDG DDNDNQELIR AKHSNIPIVS
     PQWIRACEVE KKIIGVRGFY LDADKSILKG YAFPEDTKAS ISEDQFNNSK SLEKPEEDAN
     AEAEVDNNTS DGLTNESSNV NTTTEPKEKE DDEIGEPKGS SEAPIEILEK KEDDSQLEKD
     NEKVNTPVDA PIDSIVEDTP STDNDRGTFE KDSPDSEALD NVEILDAVDG SVENIDPINE
     ELSSEKKKLE EENVLQEQDE KEKEDENDEF GEPVQAPIDT KDSLEDVPVD NEINQNQSLS
     ENPAESSNEV PIEKVVESEE PTESPIEAAQ VKTNETSDSQ TETQLNETIS EPVEINEPSE
     SQTETQLNET IGEPVEINEP SEPQTEATIS ESIEEQINPT EQQTDVTIGT LADSKIEEPS
     ETKDENDSNL SETPIQKHLE QLKNEDDLIN IIEDEESKAG TPDEIIEPKD SIISRKEDEL
     ENPLHSHNQV AKSSTSLALE ESPAVSTIQE DEGTIEENDM PADMSSLPTE QDISPDLDES
     IKVEDVSEDV SEDAVQDGTD EGSDDADAGE NESLESSNPT ATTKTQTNNK KNKNKKKKKG
     KKRK
//
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