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Database: UniProt
Entry: U6JBG8_ECHGR
LinkDB: U6JBG8_ECHGR
Original site: U6JBG8_ECHGR 
ID   U6JBG8_ECHGR            Unreviewed;      1097 AA.
AC   U6JBG8;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=FACT complex subunit {ECO:0000256|RuleBase:RU367052};
GN   Name=EGR_09023 {ECO:0000313|WBParaSite:EgrG_001138800};
GN   ORFNames=EGR_09023 {ECO:0000313|EMBL:EUB56131.1}, EgrG_001138800
GN   {ECO:0000313|EMBL:CDS20690.1};
OS   Echinococcus granulosus (Hydatid tapeworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC   Eucestoda; Cyclophyllidea; Taeniidae; Echinococcus;
OC   Echinococcus granulosus group.
OX   NCBI_TaxID=6210 {ECO:0000313|EMBL:EUB56131.1, ECO:0000313|Proteomes:UP000019149};
RN   [1] {ECO:0000313|EMBL:EUB56131.1, ECO:0000313|Proteomes:UP000019149}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24013640; DOI=10.1038/ng.2757;
RA   Zheng H., Zhang W., Zhang L., Zhang Z., Li J., Lu G., Zhu Y., Wang Y.,
RA   Huang Y., Liu J., Kang H., Chen J., Wang L., Chen A., Yu S., Gao Z.,
RA   Jin L., Gu W., Wang Z., Zhao L., Shi B., Wen H., Lin R., Jones M.K.,
RA   Brejova B., Vinar T., Zhao G., McManus D.P., Chen Z., Zhou Y., Wang S.;
RT   "The genome of the hydatid tapeworm Echinococcus granulosus.";
RL   Nat. Genet. 45:1168-1175(2013).
RN   [2] {ECO:0000313|EMBL:CDS20690.1, ECO:0000313|Proteomes:UP000492820}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23485966; DOI=10.1038/nature12031;
RA   Tsai I.J., Zarowiecki M., Holroyd N., Garciarrubio A., Sanchez-Flores A.,
RA   Brooks K.L., Tracey A., Bobes R.J., Fragoso G., Sciutto E., Aslett M.,
RA   Beasley H., Bennett H.M., Cai J., Camicia F., Clark R., Cucher M.,
RA   De Silva N., Day T.A., Deplazes P., Estrada K., Fernandez C., Holland P.W.,
RA   Hou J., Hu S., Huckvale T., Hung S.S., Kamenetzky L., Keane J.A., Kiss F.,
RA   Koziol U., Lambert O., Liu K., Luo X., Luo Y., Macchiaroli N., Nichol S.,
RA   Paps J., Parkinson J., Pouchkina-Stantcheva N., Riddiford N., Rosenzvit M.,
RA   Salinas G., Wasmuth J.D., Zamanian M., Zheng Y., Cai X., Soberon X.,
RA   Olson P.D., Laclette J.P., Brehm K., Berriman M., Garciarrubio A.,
RA   Bobes R.J., Fragoso G., Sanchez-Flores A., Estrada K., Cevallos M.A.,
RA   Morett E., Gonzalez V., Portillo T., Ochoa-Leyva A., Jose M.V., Sciutto E.,
RA   Landa A., Jimenez L., Valdes V., Carrero J.C., Larralde C.,
RA   Morales-Montor J., Limon-Lason J., Soberon X., Laclette J.P.;
RT   "The genomes of four tapeworm species reveal adaptations to parasitism.";
RL   Nature 496:57-63(2013).
RN   [3] {ECO:0000313|EMBL:CDS20690.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Aslett M.;
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|WBParaSite:EgrG_001138800}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (OCT-2020) 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; LK028581; CDS20690.1; -; Genomic_DNA.
DR   EMBL; APAU02000128; EUB56131.1; -; Genomic_DNA.
DR   AlphaFoldDB; U6JBG8; -.
DR   STRING; 6210.U6JBG8; -.
DR   EnsemblMetazoa; XM_024498272.1; XP_024347327.1; GeneID_36344738.
DR   WBParaSite; EgrG_001138800; EgrG_001138800; EgrG_001138800.
DR   OMA; YHINTIP; -.
DR   OrthoDB; 169847at2759; -.
DR   Proteomes; UP000019149; Unassembled WGS sequence.
DR   Proteomes; UP000492820; Unassembled WGS sequence.
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   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   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:UP000019149};
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..165
FT                   /note="FACT complex subunit Spt16 N-terminal lobe"
FT                   /evidence="ECO:0000259|SMART:SM01285"
FT   DOMAIN          571..731
FT                   /note="FACT complex subunit Spt16"
FT                   /evidence="ECO:0000259|SMART:SM01286"
FT   DOMAIN          850..940
FT                   /note="Histone chaperone RTT106/FACT complex subunit SPT16-
FT                   like middle"
FT                   /evidence="ECO:0000259|SMART:SM01287"
FT   REGION          432..494
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          966..1097
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        432..449
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        450..467
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        969..1053
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1054..1077
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1078..1097
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1097 AA;  124815 MW;  AD6D199BC8AE3282 CRC64;
     MTASLDVKLF ASRIKRFYEQ WESPQSNFSD VDAFLVLNGK SEDIYGKTIS TQTYFFGYEL
     QETAMLIAKK GITILSSRKK VEFLKPLNSS GVENLTFTLL TRSQDDADKA NVALLAKDFL
     SSGNGDKLGV FSKEIERNSE SEFSKSVAST LKSKAKEVVD SSLMFSQFFA AKEEVEVQYL
     RKASEVTCIL FSKHLKEKIM DVIDDDKKVS HQSLSDGCQE ALKNRDLTRG YEQEFLEICY
     DPIIQSGGSY NLKFSAENDK KPMHFGTIIC SLGVRYRSYC SNVVRTLIVN PNAKQSTYYE
     YLHNLLDWAI EQMKPGVVFS NFYNTIVNKV KVDHPELVDK LIRTFGFVTG IEFRDGNYVI
     GPKSSAVFRE GMSININLGF QDLLNEEAES EKDKHYALWL GDIVILGLGE NRTNQVLTAA
     AKRRPRAVSL YIEEDEEEEE AEGAEDENVD GEGTDAKRRK KEVSGASKDG SRPGFGGGGG
     LENGDVDGGP EALGRGHRRA ILDQKTRSEQ TAEEKRLQQR RELFQQLQVS ARNRLSGLKA
     DGETGQKAKS NVAYKGAGQM PKEDDVRKLR IFVDKKYETV ILPIFGHPTP FHISTIKNVS
     SSIEADYTYL RINFHHPGAV VGPKDASNFQ NPQATFLKEM TYRASNQRHH GETTSPSTNL
     NNAYRIIKEV LKKFRSREAE EKERANLVEQ DNLVIEPGKT AFRLRDLYIR PNIVAKRITG
     TLEAHSNGFR FTSIRGDKVD ILYNNIKHAF YQPCDGEMII LLHFNLKNAI MYGKKKQDNI
     QFYTEVGELT TDLGKSHSRM YDRDDLEAEQ REREMREQIK TAFKTFVERV ENLAKRYNLE
     FEVPFRDLGF YGCPLRTTVF MMPTSSCLVS LSEWPPFVIT LEEVELVMFE RVSLSIKTFD
     MIFVFKDYRI KPAMITSIPS NSLDHVKEWI LSCDIYYAEG VRSMNWPKLM KTIIDDPEDF
     LEQNGWAFIS PDDDDDEDED GFDSDADDES YQPSMDSDAE DDEGGGGGDE DGDGSGSEYN
     DDDDDDEEED WDAEEESSAE GSLDSDESEG KDWEELEREA IREDRKREHD DAVRAKKRHR
     SPSPRPAKKA KHHHQRR
//
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