ID M3WJL5_FELCA Unreviewed; 1047 AA.
AC M3WJL5;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=FACT complex subunit {ECO:0000256|RuleBase:RU367052};
GN Name=SUPT16H {ECO:0000313|Ensembl:ENSFCAP00000012851.4,
GN ECO:0000313|VGNC:VGNC:65846};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000012851.4, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000012851.4, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000012851.4,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000012851.4, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000012851.4,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000012851.4}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000012851.4};
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Component of the FACT complex, a general chromatin factor
CC that acts to reorganize nucleosomes. The FACT complex is involved in
CC multiple processes that require DNA as a template such as mRNA
CC elongation, DNA replication and DNA repair. During transcription
CC elongation the FACT complex acts as a histone chaperone that both
CC destabilizes and restores nucleosomal structure. It facilitates the
CC passage of RNA polymerase II and transcription by promoting the
CC dissociation of one histone H2A-H2B dimer from the nucleosome, then
CC subsequently promotes the reestablishment of the nucleosome following
CC the passage of RNA polymerase II. {ECO:0000256|RuleBase:RU367052}.
CC -!- SUBUNIT: Component of the FACT complex.
CC {ECO:0000256|RuleBase:RU367052}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU367052}.
CC Chromosome {ECO:0000256|RuleBase:RU367052}.
CC -!- SIMILARITY: Belongs to the peptidase M24 family. SPT16 subfamily.
CC {ECO:0000256|ARBA:ARBA00010779, ECO:0000256|RuleBase:RU367052}.
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DR EMBL; AANG04001761; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003987478.2; XM_003987429.4.
DR AlphaFoldDB; M3WJL5; -.
DR SMR; M3WJL5; -.
DR STRING; 9685.ENSFCAP00000012851; -.
DR PaxDb; 9685-ENSFCAP00000012851; -.
DR Ensembl; ENSFCAT00000013862.6; ENSFCAP00000012851.4; ENSFCAG00000013858.6.
DR GeneID; 101097154; -.
DR KEGG; fca:101097154; -.
DR CTD; 11198; -.
DR VGNC; VGNC:65846; SUPT16H.
DR eggNOG; KOG1189; Eukaryota.
DR GeneTree; ENSGT00390000014495; -.
DR HOGENOM; CLU_004627_0_0_1; -.
DR InParanoid; M3WJL5; -.
DR OMA; YHINTIP; -.
DR OrthoDB; 169847at2759; -.
DR Proteomes; UP000011712; Chromosome B3.
DR Bgee; ENSFCAG00000013858; Expressed in embryonic head and 10 other cell types or tissues.
DR GO; GO:0035101; C:FACT complex; IBA:GO_Central.
DR GO; GO:0031491; F:nucleosome binding; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0006337; P:nucleosome disassembly; IEA:Ensembl.
DR GO; GO:0006368; P:transcription elongation by RNA polymerase II; IBA:GO_Central.
DR CDD; cd01091; CDC68-like; 1.
DR Gene3D; 2.30.29.150; -; 1.
DR Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 1.
DR Gene3D; 3.40.350.10; Creatinase/prolidase N-terminal domain; 1.
DR Gene3D; 2.30.29.210; FACT complex subunit Spt16p/Cdc68p; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR029148; FACT-Spt16_Nlobe.
DR InterPro; IPR013953; FACT_Spt16.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR013719; RTT106/SPT16-like_middle_dom.
DR InterPro; IPR040258; Spt16.
DR InterPro; IPR048969; SPT16_C.
DR InterPro; IPR033825; Spt16_M24.
DR PANTHER; PTHR13980; CDC68 RELATED; 1.
DR PANTHER; PTHR13980:SF15; FACT COMPLEX SUBUNIT SPT16; 1.
DR Pfam; PF14826; FACT-Spt16_Nlob; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR Pfam; PF08512; Rttp106-like_middle; 1.
DR Pfam; PF08644; SPT16; 1.
DR Pfam; PF21091; SPT16_C; 1.
DR SMART; SM01285; FACT-Spt16_Nlob; 1.
DR SMART; SM01287; Rtt106; 1.
DR SMART; SM01286; SPT16; 1.
DR SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
PE 3: Inferred from homology;
KW Chromosome {ECO:0000256|ARBA:ARBA00022454, ECO:0000256|RuleBase:RU367052};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU367052};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU367052};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW ECO:0000256|RuleBase:RU367052};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU367052};
KW Reference proteome {ECO:0000313|Proteomes:UP000011712};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU367052};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW ECO:0000256|RuleBase:RU367052}.
FT DOMAIN 5..168
FT /note="FACT complex subunit Spt16 N-terminal lobe"
FT /evidence="ECO:0000259|SMART:SM01285"
FT DOMAIN 529..689
FT /note="FACT complex subunit Spt16"
FT /evidence="ECO:0000259|SMART:SM01286"
FT DOMAIN 806..896
FT /note="Histone chaperone RTT106/FACT complex subunit SPT16-
FT like middle"
FT /evidence="ECO:0000259|SMART:SM01287"
FT REGION 492..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 918..1047
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 929..971
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 972..1018
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1047 AA; 119959 MW; 9F0B0D5446FB10F4 CRC64;
MAVTLDKDAY YRRVKRLYSN WRKGEDEYAN VDAIVVSVGV DEEIVYAKST ALQTWLFGYE
LTDTIMVFCD DKIIFMASKK KVEFLKQIAN TKGNENANGA PAITLLIREK NESNKSSFDK
MIEAIKESKN GKKIGVFSKD KFPGEFMKNW NDCLNKEGFD KIDISAVVAY TIAVKEDGEL
NLMKKAASIT SEVFNKFFKE RVMEIVDADE KVRHSKLAES VEKAIEEKKY LAGADPSTVE
MCYPPIIQSG GNYNLKFSVV SDKNHMHFGA ITCAMGIRFK SYCSNLVRTL MVDPSQEVQE
NYNFLLQLQE ELLKELRHGV KICDVYNAVM DVVKKQKPEL LNKITKNLGF GMGIEFREGS
LVINSKNQYK LKKGMVFSIN LGFSDLTNKE GKKPEEKTYA LFIGDTVLVD EDGPATVLTS
VKKKVKNVGI FLKNEDEEEE EEEKDEAEDL LGRGSRAALL TERTRNEMTA EEKRRAHQKE
LAAQLNEEAK RRLTEQKGEQ QIQKARKSNV SYKNPSLMPK EPHIREMKIY IDKKYETVIM
PVFGIATPFH IATIKNISMS VEGDYTYLRI NFYCPGSALG RNEGNIFPNP EATFVKEITY
RASNMKAPGE QTVPALNLQN AFRIIKEVQK RYKTREAEEK EKEGIVKQDS LVINLNRSNP
KLKDLYIRPN IAQKRMQGSL EAHVNGFRFT SVRGDKVDIL YNNIKHALFQ PCDGEMIIVL
HFHLKNAIMF GKKRHTDVQF YTEVGEITTD LGKHQHMHDR DDLYAEQMER EMRHKLKTAF
KNFIEKVEAL TKEELEFEVP FRDLGFNGAP YRSTCLLQPT SSALVNATEW PPFVVTLDEV
ELIHFERVQF HLKNFDMVIV YKDYSKKVTM INAIPVASLD PIKEWLNSCD LKYTEGVQSL
NWTKIMKTIV DDPEGFFEQG GWSFLEPEGE GSDAEEGDSE SEIEDETFNP SEDDYEEEEE
DSDEDYSSEA EESDYSKESL GSEEESGKDW DELEEEARKA DRESRYEEEE EQSRSMSRKR
KASVHSSGRG SNRGSRHSSA PPKKKRK
//
