SPT2_XENTR
ID SPT2_XENTR Reviewed; 778 AA.
AC Q0V9A3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Protein SPT2 homolog;
DE AltName: Full=SPT2 domain-containing protein 1;
GN Name=spty2d1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=N6; TISSUE=Oviduct;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Histone chaperone that stabilizes pre-existing histone
CC tetramers and regulates replication-independent histone exchange on
CC chromatin. Required for normal chromatin refolding in the coding region
CC of transcribed genes, and for the suppression of spurious
CC transcription. Binds DNA and histones and promotes nucleosome assembly
CC (in vitro). Facilitates formation of tetrameric histone complexes
CC containing histone H3 and H4 (By similarity). Modulates RNA polymerase
CC 1-mediated transcription (By similarity). Binds DNA, with a preference
CC for branched DNA species, such as Y-form DNA and Holliday junction DNA
CC (By similarity). {ECO:0000250|UniProtKB:E1BUG7,
CC ECO:0000250|UniProtKB:Q68D10}.
CC -!- SUBUNIT: Interacts with histones. Interacts with a heterotetrameric
CC complex formed by histone H3 and H4, especially when the histone
CC tetramer is not bound to DNA. {ECO:0000250|UniProtKB:Q68D10}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:E1BUG7}.
CC -!- DOMAIN: The acidic C-terminal domain mediates interaction with histone
CC H3/H4 complexes. {ECO:0000250|UniProtKB:Q68D10}.
CC -!- SIMILARITY: Belongs to the SPT2 family. {ECO:0000305}.
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DR EMBL; BC121680; AAI21681.1; -; mRNA.
DR RefSeq; NP_001072434.1; NM_001078966.1.
DR AlphaFoldDB; Q0V9A3; -.
DR SMR; Q0V9A3; -.
DR PaxDb; Q0V9A3; -.
DR PRIDE; Q0V9A3; -.
DR GeneID; 779888; -.
DR KEGG; xtr:779888; -.
DR CTD; 144108; -.
DR Xenbase; XB-GENE-5939956; spty2d1.
DR eggNOG; ENOG502QWHS; Eukaryota.
DR HOGENOM; CLU_516363_0_0_1; -.
DR InParanoid; Q0V9A3; -.
DR OrthoDB; 1092455at2759; -.
DR Proteomes; UP000008143; Chromosome 4.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR GO; GO:0140713; F:histone chaperone activity; ISS:UniProtKB.
DR GO; GO:0001042; F:RNA polymerase I core binding; ISS:UniProtKB.
DR GO; GO:0031507; P:heterochromatin assembly; ISS:UniProtKB.
DR GO; GO:0043486; P:histone exchange; IBA:GO_Central.
DR GO; GO:0006334; P:nucleosome assembly; ISS:UniProtKB.
DR GO; GO:0010847; P:regulation of chromatin assembly; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
DR InterPro; IPR013256; Chromatin_SPT2.
DR Pfam; PF08243; SPT2; 1.
DR SMART; SM00784; SPT2; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; DNA-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..778
FT /note="Protein SPT2 homolog"
FT /id="PRO_0000315740"
FT REGION 1..665
FT /note="Important for interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:Q68D10"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 50..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 639..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 666..778
FT /note="Important for interaction with histones"
FT /evidence="ECO:0000250|UniProtKB:Q68D10"
FT COILED 44..83
FT /evidence="ECO:0000255"
FT COILED 193..221
FT /evidence="ECO:0000255"
FT COILED 735..778
FT /evidence="ECO:0000255"
FT COMPBIAS 50..88
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..148
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..231
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..292
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..566
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..584
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..672
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 778 AA; 81318 MW; 7368C5722A7D65C2 CRC64;
MDFHSVLKMA AAKPGSDGIA KRYSLAVGPP KKDPKVKGVD SAAVQAFLRK KDEESRRKET
VEKRKKEDLL AKRKELKHDR KARAMASRTK DNFKGYNGIP IEEKPRKRKR SGTEEDQNDN
MAAEGEEYMT EEELYEYSQS ESEQEEEEEL PPQKVPKPAP GKKPPTPALN FNDLLRLAER
KQYEPVEVVR PVKKEERLRT AEELKELEFL ERKAQKADRK DPKRNEQLVK VSKGSGDKYS
SLKGTHSGNS KSSSTEQNGT IRKSSSDTGS RTEKSGSVFH TKESKKPSSA KDLGGKGSRP
NVTGDGKDRH SSSQPSAASN SAFGRPSGSA RPSGSSGPGR PLGGSGSSSG KSTGGSASGS
ARSVGGSGSG SGKPMGGSGS GKPIGGLHSS HGSGKPTGGT GSGSGKPTGA SGSGSGKPTG
SSGSAKSVRE SGSGSRSVRE SGSGSRSVRE SGSGSGSARS VRESGSGSGS ARSVRESGSG
SGSARSVRES GSAKQAGGPG SGRALGSGSS FARPSSNSSP APGKPAAGSG SARPSSSGTP
RSSSMGHSTS NSSRQPSSSG AVRPSSGPPT GATPKGPSPR PGAGPTSVRP NSTSVPGSAR
SSLGSGPGRP VAASATGQLA PAKPKCTVVA ETISSKNFVP KSINGHMNGI RTAAPPGHRP
AMRPPGPPLP PITSSYKRRI DDDDDYDSEM DDFIDDGGEC QDEISKHIRE IFGYDRTKYR
DESDYALRYM ESTFREQQKE EARSLRLGIQ EDLEELQREE EELKRKAKQL KAAKKMSR
