ID   KAP4_CRIFA              Reviewed;         128 AA.
AC   Q07053;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   31-MAY-2011, sequence version 2.
DT   25-MAY-2022, entry version 47.
DE   RecName: Full=Kinetoplast-associated protein 4;
DE   AltName: Full=Histone H1-like protein p16;
DE   Flags: Precursor;
GN   Name=KAP4;
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 [MRNA] OF 1-24, 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}. Mitochondrion
CC       matrix {ECO:0000269|PubMed:8446592, ECO:0000269|PubMed:8552084}.
CC       Note=Present both within the kDNA disk and in the mitochondrial matrix
CC       at opposite edges of the kDNA disk. {ECO:0000269|PubMed:8552084}.
CC   -!- SIMILARITY: Belongs to the KAP family. {ECO:0000305}.
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DR   EMBL; S56498; AAB25701.1; -; mRNA.
DR   PIR; JC6092; JC6092.
DR   AlphaFoldDB; Q07053; -.
DR   SMR; Q07053; -.
DR   VEuPathDB; TriTrypDB:CFAC1_280066300; -.
DR   GO; GO:0020023; C:kinetoplast; IDA:UniProtKB.
DR   GO; GO:0005759; C:mitochondrial matrix; 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_0000409304"
FT   CHAIN           11..128
FT                   /note="Kinetoplast-associated protein 4"
FT                   /id="PRO_0000409305"
FT   REGION          60..87
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        60..79
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   128 AA;  14590 MW;  D044525C19841B48 CRC64;
     MLRFVPRRLA IGAYTLFMME QKNNPKLKGL KIADRGKMTS KLYKALNPND KAALEKRAAA
     HPGFKRKEKE PKELKAAKAA KTSTPRAPSE YAKFVQANIG RFEKLPHLDR MKAVAKLWKQ
     QQMRTGKP