ID F7EL37_XENTR Unreviewed; 1035 AA.
AC F7EL37;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 3.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=FACT complex subunit {ECO:0000256|RuleBase:RU367052};
GN Name=supt16h {ECO:0000313|Ensembl:ENSXETP00000037495,
GN ECO:0000313|RefSeq:NP_001362206.1,
GN ECO:0000313|Xenbase:XB-GENE-979305};
GN Synonyms=cdc68 {ECO:0000313|RefSeq:NP_001362206.1}, fact
GN {ECO:0000313|RefSeq:NP_001362206.1}, factp140
GN {ECO:0000313|RefSeq:NP_001362206.1}, spt16/cdc68
GN {ECO:0000313|RefSeq:NP_001362206.1};
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 {ECO:0000313|Ensembl:ENSXETP00000037495};
RN [1] {ECO:0000313|Ensembl:ENSXETP00000037495}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nigerian {ECO:0000313|Ensembl:ENSXETP00000037495};
RX PubMed=20431018; DOI=10.1126/science.1183670;
RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT "The genome of the Western clawed frog Xenopus tropicalis.";
RL Science 328:633-636(2010).
RN [2] {ECO:0000313|Ensembl:ENSXETP00000037495}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUN-2011) to UniProtKB.
RN [3] {ECO:0000313|RefSeq:NP_001362206.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-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}.
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 RefSeq; NP_001362206.1; NM_001375277.1.
DR STRING; 8364.ENSXETP00000037495; -.
DR Ensembl; ENSXETT00000037495; ENSXETP00000037495; ENSXETG00000017204.
DR KEGG; xtr:549984; -.
DR AGR; Xenbase:XB-GENE-979305; -.
DR Xenbase; XB-GENE-979305; supt16h.
DR eggNOG; KOG1189; Eukaryota.
DR HOGENOM; CLU_004627_0_0_1; -.
DR OMA; YHINTIP; -.
DR OrthoDB; 169847at2759; -.
DR TreeFam; TF300341; -.
DR Reactome; R-XTR-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-XTR-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-XTR-75955; RNA Polymerase II Transcription Elongation.
DR Proteomes; UP000008143; Chromosome 1.
DR Bgee; ENSXETG00000017204; Expressed in ovary and 16 other cell types or tissues.
DR GO; GO:0035101; C:FACT complex; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
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:UP000008143};
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..169
FT /note="FACT complex subunit Spt16 N-terminal lobe"
FT /evidence="ECO:0000259|SMART:SM01285"
FT DOMAIN 531..691
FT /note="FACT complex subunit Spt16"
FT /evidence="ECO:0000259|SMART:SM01286"
FT DOMAIN 808..898
FT /note="Histone chaperone RTT106/FACT complex subunit SPT16-
FT like middle"
FT /evidence="ECO:0000259|SMART:SM01287"
FT REGION 488..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 919..1035
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..504
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..520
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 933..993
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 994..1020
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1021..1035
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1035 AA; 118480 MW; 210F69EB789DC3E6 CRC64;
MAVTLDKEAY YRRIKRFYGN WKKGEDEFAN VDAIVVSVGV DEEIVYAKST ALQTWLFGYE
LTDTIMVFCE EKIIFMASKK KVEFLKQIAN TKGNENANGT PAITLLVREK QNEANKANFE
KVIEAIKGSK KGKYIGVFIK DKFPGDYMKS WYDTLNKEGF DKVDISASLA YTIAVKEDGE
LNLMKKAATI TSDVFSKFFK DRVMEIVDAD EKVRHSKLAE SVEKAIEDKK YLGGTDPSTI
EMCYPPIIQS GGNYNLKFSV VSDKNHMHFG AITCAMGIRY KSYCSNLVRT LMVDPTQEMQ
DNYNFLLQLQ EELLKELKHG AKICDAYHII MDQVKKQKPD LLSKITKNLG FAMGIEFREG
SLVINNKNQY KLKKGMVFSV HLGLSELNNK AGKKPEEKTY ALFVGDTVLV NEEGAATVLT
HVKKKVKNVG IFLKKEDDEE EEEDKDEAQD ILGRGARSAA LLTERTRNEM TAEEKRRTHQ
KELATQLNDE AKRRLTEQKG EQQTLKARKS NVSYKNASQM PKESEIREMK IYIDKKYETV
IMPVFGIATP FHIATIKNIS MSVEGDYTYL RINFFCPGSA LGRNEGNIFP NPEATFVKEI
TYRASNVKTP GDPSVPSLNL QNAFRIIKEV QKRYKTREAE EKEKEGIVKQ DSLVINLNRS
NPKLKDLYIR PNIAQKRMQG SLEAHVNGFR FTSVRGDKVD ILYNNIKHAI FQPCDGEMII
VLHFHLKNAI MFGKKRHTDV QFYTEVGEIT TDLGKHQHMH DRDDLYAEQL EREMRHKLKT
AFKNFIEKVE SLTKEDLEFE VPFRDLGFNG APYRSTCLLQ PTSSALVNTT EWPPFVVTLD
EVELVHFERV QFHLKNFDMV IVYKEYGKKV TMINAIPVAS LDPIKEWLNS CDIKYTEGVQ
SLNWTKIMKT IVDDPEGFFE QGGWSFLEPE GEGSGAEEGE SESEMEDETF NPSEDEYEEE
EEDSDEDYSD ETEESVGSEE SLGTDEESGK DWDELEEEAR KADRESRYEE EEEQKGGKKR
KVHAPAPNPS KKRKK
//
