ID A0AAF0P885_9EUCA Unreviewed; 109 AA. AC A0AAF0P885; DT 29-MAY-2024, integrated into UniProtKB/TrEMBL. DT 29-MAY-2024, sequence version 1. DT 27-NOV-2024, entry version 4. DE RecName: Full=Histone H3 {ECO:0000256|RuleBase:RU004471}; DE Flags: Fragment; GN Name=histone H3 {ECO:0000313|EMBL:WMS59320.1}; OS Tenuipotamon tonghaiense. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea; OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Brachyura; OC Eubrachyura; Potamoidea; Potamidae; Tenuipotamon. OX NCBI_TaxID=2875582 {ECO:0000313|EMBL:WMS59320.1}; RN [1] {ECO:0000313|EMBL:WMS59320.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=THLS {ECO:0000313|EMBL:WMS59320.1}; RA Shi B., Pan D., Sun H.; RL Submitted (SEP-2023) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:WMS59320.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=THLS {ECO:0000313|EMBL:WMS59320.1}; RX PubMed=37898294; RA Shi B.Y., Pan D., Zhang K.Q., Gu T.Y., Yeo D.C.J., Ng P.K.L., RA Cumberlidge N., Sun H.Y.; RT "Diversification of freshwater crabs on the sky islands in the Hengduan RT Mountains Region, China."; RL Mol. Phylogenet. Evol. 190:0-0(2024). CC -!- SUBUNIT: The nucleosome is a histone octamer containing two molecules CC each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and CC two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of CC DNA. {ECO:0000256|RuleBase:RU004471}. CC -!- SIMILARITY: Belongs to the histone H3 family. CC {ECO:0000256|ARBA:ARBA00010343, ECO:0000256|RuleBase:RU004471}. 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 EMBL; OR515471; WMS59320.1; -; mRNA. DR SMR; A0AAF0P885; -. DR GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro. DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro. DR FunFam; 1.10.20.10:FF:000001; Histone H3; 1. DR Gene3D; 1.10.20.10; Histone, subunit A; 1. DR InterPro; IPR009072; Histone-fold. DR InterPro; IPR007125; Histone_H2A/H2B/H3. DR InterPro; IPR000164; Histone_H3/CENP-A. DR PANTHER; PTHR11426; HISTONE H3; 1. DR PANTHER; PTHR11426:SF274; HISTONE H3.1T; 1. DR Pfam; PF00125; Histone; 1. DR PRINTS; PR00622; HISTONEH3. DR SMART; SM00428; H3; 1. DR SUPFAM; SSF47113; Histone-fold; 1. DR PROSITE; PS00322; HISTONE_H3_1; 1. DR PROSITE; PS00959; HISTONE_H3_2; 1. PE 2: Evidence at transcript level; KW Chromosome {ECO:0000256|RuleBase:RU004471}; KW DNA-binding {ECO:0000256|RuleBase:RU004471}; KW Nucleosome core {ECO:0000256|RuleBase:RU004471}; KW Nucleus {ECO:0000256|RuleBase:RU004471}. FT DOMAIN 2..109 FT /note="Histone H2A/H2B/H3" FT /evidence="ECO:0000259|Pfam:PF00125" FT REGION 1..35 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:WMS59320.1" FT NON_TER 109 FT /evidence="ECO:0000313|EMBL:WMS59320.1" SQ SEQUENCE 109 AA; 12294 MW; 789F4869FFC39A60 CRC64; RKSTGGKAPR KQLATKAARK SAPATGGVKK PHRYRPGTVA LREIRRYQKS TELLIRKLPF QRLVREIAQD FKTDLRFQSS AVMALQEASE AYLVGLFEDT NLCAIHAKR //