ID   KAP21_CRIFA             Reviewed;         130 AA.
AC   Q9TY83;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 47.
DE   RecName: Full=kinetoplast-associated protein 2-1;
DE   AltName: Full=Histone H1-like protein p18-1;
DE   Flags: Precursor;
GN   Name=KAP2-1;
OS   Crithidia fasciculata.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Crithidia.
OX   NCBI_TaxID=5656;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], DNA-BINDING, FUNCTION, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=8552084; DOI=10.1128/mcb.16.2.564;
RA   Xu C.W., Hines J.C., Engel M.L., Russell D.G., Ray D.S.;
RT   "Nucleus-encoded histone H1-like proteins are associated with kinetoplast
RT   DNA in the trypanosomatid Crithidia fasciculata.";
RL   Mol. Cell. Biol. 16:564-576(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9297699; DOI=10.1016/s0166-6851(97)00099-6;
RA   Hines J.C., Ray D.S.;
RT   "Tandem arrangement of two genes encoding kinetoplast-associated H1
RT   histone-like proteins.";
RL   Mol. Biochem. Parasitol. 89:41-49(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-17, PROTEIN SEQUENCE OF 10-24, DNA-BINDING,
RP   AND SUBCELLULAR LOCATION.
RX   PubMed=8446592; DOI=10.1073/pnas.90.5.1786;
RA   Xu C., Ray D.S.;
RT   "Isolation of proteins associated with kinetoplast DNA networks in vivo.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:1786-1789(1993).
CC   -!- FUNCTION: Histone H1-like DNA-binding protein involved in the
CC       organization and segregation of kinetoplast DNA (kDNA). The
CC       mitochondrial DNA of kinetoplastid protozoa consists of about 5,000
CC       minicircles and 20 to 30 maxicircles. These circular DNAs are held
CC       together by catenation into a highly organized compact disk structure
CC       referred to as a kinetoplast DNA (kDNA) network. Binds preferentially
CC       to a specific fragment of minicircle DNA and is able to compact kDNA
CC       networks through DNA charge neutralization and condensation.
CC       {ECO:0000269|PubMed:8552084}.
CC   -!- SUBUNIT: Associates with the kinetoplast DNA network.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix, kinetoplast
CC       {ECO:0000269|PubMed:8446592, ECO:0000269|PubMed:8552084}.
CC   -!- SIMILARITY: Belongs to the KAP family. {ECO:0000305}.
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DR   EMBL; AF008944; AAC47741.1; -; Genomic_DNA.
DR   PIR; JC6090; JC6090.
DR   AlphaFoldDB; Q9TY83; -.
DR   SMR; Q9TY83; -.
DR   VEuPathDB; TriTrypDB:CFAC1_300049900; -.
DR   GO; GO:0020023; C:kinetoplast; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR   Gene3D; 1.10.30.10; -; 1.
DR   InterPro; IPR009071; HMG_box_dom.
DR   InterPro; IPR036910; HMG_box_dom_sf.
DR   SMART; SM00398; HMG; 1.
DR   SUPFAM; SSF47095; SSF47095; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; DNA-binding; Kinetoplast; Mitochondrion.
FT   PROPEP          1..10
FT                   /id="PRO_0000409298"
FT   CHAIN           11..130
FT                   /note="kinetoplast-associated protein 2-1"
FT                   /id="PRO_0000409299"
FT   REGION          89..130
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        89..109
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        110..130
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   130 AA;  14857 MW;  E47255CAD5BE8808 CRC64;
     MLRRTVSNFA MSPYMLFISD LAKTGKLKGI RTPGKFVGKK YRQLSAKEKA ALQQRAKQAS
     TPAMTAYRRM AHREMSNKSV PIEQRRANLT KKWNETKQAQ REKAQKAQKK TKSAKSKVKK
     AAKKSKKSKK