ID A0A183R464_9TREM Unreviewed; 136 AA. AC A0A183R464; DT 07-SEP-2016, integrated into UniProtKB/TrEMBL. DT 07-SEP-2016, sequence version 1. DT 05-JUL-2017, entry version 7. DE RecName: Full=Histone H3 {ECO:0000256|RuleBase:RU004471}; OS Schistosoma rodhaini. OC Eukaryota; Metazoa; Platyhelminthes; Trematoda; Digenea; Strigeidida; OC Schistosomatoidea; Schistosomatidae; Schistosoma. OX NCBI_TaxID=6188 {ECO:0000313|Proteomes:UP000050792, ECO:0000313|WBParaSite:SROB_0001075601-mRNA-1}; RN [1] {ECO:0000313|Proteomes:UP000050792, ECO:0000313|WBParaSite:SROB_0001075601-mRNA-1, ECO:0000313|WBParaSite:SROB_0001417601-mRNA-1} RP NUCLEOTIDE SEQUENCE. RG Helminth Genomes Consortium; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|WBParaSite:SROB_0001075601-mRNA-1, ECO:0000313|WBParaSite:SROB_0001417601-mRNA-1} RP IDENTIFICATION. RG WormBaseParasite; RL Submitted (JUN-2016) to UniProtKB. CC -!- SUBUNIT: The nucleosome is a histone octamer containing two CC molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 CC heterotetramer and two H2A-H2B heterodimers. The octamer wraps CC approximately 147 bp of DNA. {ECO:0000256|RuleBase:RU004471}. CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|SAAS:SAAS00690744}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|SAAS:SAAS00690742}. CC -!- SIMILARITY: Belongs to the histone H3 family. CC {ECO:0000256|RuleBase:RU004471, ECO:0000256|SAAS:SAAS00690741}. 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 ProteinModelPortal; A0A183R464; -. DR WBParaSite; SROB_0001075601-mRNA-1; SROB_0001075601-mRNA-1; SROB_0001075601. DR WBParaSite; SROB_0001417601-mRNA-1; SROB_0001417601-mRNA-1; SROB_0001417601. DR Proteomes; UP000050792; Genome assembly. DR GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro. 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. DR PROSITE; PS00322; HISTONE_H3_1; 1. DR PROSITE; PS00959; HISTONE_H3_2; 1. PE 3: Inferred from homology; KW Chromosome {ECO:0000256|SAAS:SAAS00142380}; KW Complete proteome {ECO:0000313|Proteomes:UP000050792}; KW DNA-binding {ECO:0000256|SAAS:SAAS00142373}; KW Nucleosome core {ECO:0000256|RuleBase:RU004471}; KW Nucleus {ECO:0000256|RuleBase:RU004471, KW ECO:0000256|SAAS:SAAS00142374}; KW Reference proteome {ECO:0000313|Proteomes:UP000050792}. FT DOMAIN 1 132 Histone. {ECO:0000259|Pfam:PF00125}. SQ SEQUENCE 136 AA; 15344 MW; B278508EA512770B CRC64; MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RYRPGTVALR EIRRYQKSTE LLIRKLPFQR LVREIAQDFK TDLRFQSSAV SALQEASEAY LVGLFEDTNL CAIHAKRVTI MPKDIQLARR IRGERA //