ID   HCP3L_CAEBR             Reviewed;         345 AA.
AC   A8XA80;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Histone H3-like centromeric protein cpar-1;
DE   AltName: Full=CENP-A-related protein 1;
DE   AltName: Full=Centromeric protein A related {ECO:0000250|UniProtKB:P34440};
GN   Name=cpar-1 {ECO:0000312|EMBL:CAP29548.1}; ORFNames=CBG10032;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1] {ECO:0000312|EMBL:CAP29548.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16 {ECO:0000312|EMBL:CAP29548.1};
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
CC   -!- FUNCTION: Histone H3-like variant which exclusively replaces
CC       conventional H3 in the nucleosome core of centromeric chromatin at the
CC       inner plate of the kinetochore. Required for recruitment and assembly
CC       of kinetochore proteins, mitotic progression and chromosome
CC       segregation. May serve as an epigenetic mark that propagates centromere
CC       identity through replication and cell division. Not required for
CC       chromosome segregation during meiosis. {ECO:0000250|UniProtKB:P34440}.
CC   -!- SUBUNIT: Forms a nucleosome-like histone octamer containing two
CC       molecules each of H2A, H2B, cpar-1 and H4 assembled in one cpar-1-H4
CC       heterotetramer and two H2A-H2B heterodimers.
CC       {ECO:0000250|UniProtKB:P49450}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P34440}.
CC       Chromosome {ECO:0000250|UniProtKB:P34440}. Note=Localizes to
CC       chromosomes during meiotic prometaphase I and metaphase I. Upon
CC       cleavage at the onset of anaphase I, the C-terminus remains localized
CC       to chromosomes. The cleaved form transiently associates with chromosome
CC       but not centromeres during embryonic mitosis.
CC       {ECO:0000250|UniProtKB:P34440}.
CC   -!- PTM: Cleaved at the onset of meiotic anaphase I, likely by separase
CC       sep-1. {ECO:0000250|UniProtKB:P34440}.
CC   -!- SIMILARITY: Belongs to the histone H3 family. {ECO:0000255}.
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DR   EMBL; HE601459; CAP29548.1; -; Genomic_DNA.
DR   RefSeq; XP_002641699.1; XM_002641653.1.
DR   AlphaFoldDB; A8XA80; -.
DR   SMR; A8XA80; -.
DR   STRING; 6238.CBG10032; -.
DR   GeneID; 8583693; -.
DR   KEGG; cbr:CBG_10032; -.
DR   CTD; 8583693; -.
DR   WormBase; CBG10032; CBP39652; WBGene00031517; Cbr-cpar-1.
DR   eggNOG; KOG1745; Eukaryota.
DR   HOGENOM; CLU_071908_0_0_1; -.
DR   InParanoid; A8XA80; -.
DR   OMA; NIDITHR; -.
DR   OrthoDB; 1778056at2759; -.
DR   Proteomes; UP000008549; Chromosome III.
DR   GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR   GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR   Gene3D; 1.10.20.10; -; 1.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR007125; Histone_H2A/H2B/H3.
DR   InterPro; IPR000164; Histone_H3/CENP-A.
DR   PANTHER; PTHR11426; PTHR11426; 1.
DR   Pfam; PF00125; Histone; 1.
DR   PRINTS; PR00622; HISTONEH3.
DR   SMART; SM00428; H3; 1.
DR   SUPFAM; SSF47113; SSF47113; 1.
PE   3: Inferred from homology;
KW   Chromosome; DNA-binding; Nucleosome core; Nucleus; Reference proteome.
FT   CHAIN           1..345
FT                   /note="Histone H3-like centromeric protein cpar-1"
FT                   /id="PRO_0000368210"
FT   REGION          117..246
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          263..340
FT                   /note="H3-like"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        117..145
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        146..164
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        165..187
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        188..235
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            128..129
FT                   /note="Cleavage; by sep-1"
FT                   /evidence="ECO:0000250|UniProtKB:P34440"
SQ   SEQUENCE   345 AA;  41344 MW;  DD1C3741BE558FD4 CRC64;
     MYHHDSGPHI EEVFDPPSRR TMMQEIETHP DVIAFGKKLR KIKNQPESTF LSSADRMEEI
     IDAFRDQIAK WEEEEELNEP CEYRQLKIEI FTQKKIEYQR KNNLAVDEFY KKRNLKNHSN
     RKPLEESRRR EEPRDRVHES NIDITHRGDS TSLNHYSRHH YSQRQSQSSR FERERESDEE
     EENSQPIQRY RSRSPKPSYS YNQSTMQQSQ RDDTNVYHRS HQSTSQPPQV RMRSGKSRVT
     KTHNRKFRPG QKALAEIRKY QKSTDMLIQK APFVRLVHEI IREQTYKSQD YRIRADALMA
     LQEAAEAFMV EMFEGSVLIC NHAKRVTLMP TDIQLYRRLC LRNLS