DnaJ homolog subfamily C member 9 (HDJC9) (DnaJ protein SB73)
1_MGLLD 6_ LCEEV 11_ FGTAD 16_ LYRVL 21_ GVRRE 26_ ASDGE 31_ VRRGY 36_ HKVSL 41_ QVHPD 46_ RVGEG 51_ DKEDA 56_ TRRFQ 61_ ILGKV 66_ YSVLS 71_ DREQR 76_ AVYDE 81_ QGTVD 86_ EDSPV 91_ LTQDR 96_ DWEAY 101_ WRLLF 106_ KKISL 111_ EDIQA 116_ FEKTY 121_ KGSEE 126_ ELADI 131_ KQAYL 136_ DFKGD 141_ MDQIM 146_ ESVLC 151_ VQYTE 156_ EPRIR 161_ NIIQQ 166_ AIDAG 171_ EVPSY 176_ NAFVK 181_ ESKQK 186_ MNARK 191_ RRAQE 196_ EAKEA 201_ EMSRK 206_ ELGLD 211_ EGVDS 216_ LKAAI 221_ QSRQK 226_ DRQKE 231_ MDNFL 236_ AQMEA 241_ KYCKS 246_ SKGGG 251_KKSAL
1: Acts as a dual histone chaperone and heat shock co-chaperone (PubMed:33857403). As a histone chaperone, forms a co-chaperone complex with MCM2 and histone H3-H4 heterodimers; and may thereby assist MCM2 in histone H3-H4 heterodimer recognition and facilitate the assembly of histones into nucleosomes (PubMed:33857403). May also act as a histone co-chaperone together with TONSL (PubMed:33857403). May recruit histone chaperones ASF1A, NASP and SPT2 to histone H3-H4 heterodimers (PubMed:33857403). Also plays a role as co-chaperone of the HSP70 family of molecular chaperone proteins, such as HSPA1A, HSPA1B and HSPA8 (PubMed:17182002, PubMed:33857403). As a co-chaperone, may play a role in the recruitment of HSP70-type molecular chaperone machinery to histone H3-H4 substrates, thereby maintaining the histone structural integrity (PubMed:33857403). Exhibits activity to assemble histones onto DNA in vitro (PubMed:33857403)