ID A0A1R3IUH0_COCAP Unreviewed; 1070 AA.
AC A0A1R3IUH0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=FACT complex subunit {ECO:0000256|RuleBase:RU367052};
GN ORFNames=CCACVL1_09719 {ECO:0000313|EMBL:OMO86226.1};
OS Corchorus capsularis (Jute).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Grewioideae; Apeibeae; Corchorus.
OX NCBI_TaxID=210143 {ECO:0000313|EMBL:OMO86226.1, ECO:0000313|Proteomes:UP000188268};
RN [1] {ECO:0000313|EMBL:OMO86226.1, ECO:0000313|Proteomes:UP000188268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. CVL-1 {ECO:0000313|Proteomes:UP000188268};
RC TISSUE=Whole seedling {ECO:0000313|EMBL:OMO86226.1};
RA Alam M., Haque M.S., Islam M.S., Emdad E.M., Islam M.M., Ahmed B.,
RA Halim A., Hossen Q.M.M., Hossain M.Z., Ahmed R., Khan M.M., Islam R.,
RA Rashid M.M., Khan S.A., Rahman M.S., Alam M.;
RT "Corchorus capsularis genome sequencing.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OMO86226.1}.
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DR EMBL; AWWV01009495; OMO86226.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R3IUH0; -.
DR STRING; 210143.A0A1R3IUH0; -.
DR EnsemblPlants; OMO86226; OMO86226; CCACVL1_09719.
DR Gramene; OMO86226; OMO86226; CCACVL1_09719.
DR OMA; YHINTIP; -.
DR OrthoDB; 169847at2759; -.
DR Proteomes; UP000188268; 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 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:UP000188268};
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 24..191
FT /note="FACT complex subunit Spt16 N-terminal lobe"
FT /evidence="ECO:0000259|SMART:SM01285"
FT DOMAIN 555..709
FT /note="FACT complex subunit Spt16"
FT /evidence="ECO:0000259|SMART:SM01286"
FT DOMAIN 834..924
FT /note="Histone chaperone RTT106/FACT complex subunit SPT16-
FT like middle"
FT /evidence="ECO:0000259|SMART:SM01287"
FT REGION 504..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 957..1070
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 980..1016
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1017..1044
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1070 AA; 120485 MW; E3791B25B6FDB9B7 CRC64;
MADRNRNVKP TNGKPPVAAN PYAINLDNFS KRLKIFYSHW NKNNTALWGA SCALAIATPP
VSEDLRYLKS SALNIWLLGY EFPETIMVFL KKQIHLLCSQ KKASLLDVVK KSAREAVGVE
VVIHVKAKGD DGTGLMDSIF RAISSQTNSG DHDVPVVGYI SRETPEGKLL ETWDEKLKKA
NFELSDVTNG FSDLFAVKDE TELTNVKKAA FLTSSVMRQF VVPKLEKVID EERKVSHSAL
MDDTEKTILE PARIKVKLKA ENIDICYPPI FQSGGEFDLK PSASSNDENL YYDSTSVIIC
ALGSRYNSYC SNIARTFLID ANATQSKAYE VLLKAQEAAI GALKSGNRVN SVYQAAVAVV
EKDAPELAAN LTKTAGTGIG LEFRESGLSL NAKNDRTLKT GMVFNVSLGF QNLHTDTKNP
KTQKYSVLLA DTVIVGEKVP GILTSKSSKA VKDVAYSFNE DDEEEEKLKV KAVDNGNEAL
FSKTTLRSDH HEMSKEELRR QHQAELARQK NEETARRLAG GGSMGSDHRG AVKTVGDLIA
YKNVNDLPPP RDLMIQVDQK NEAILLPIYG SMVPFHVATV KSVSSQQDSN RTSYIRIIFN
VPGTPFSPHD ANSLKFQGSI YLKEVSFRSK DSRHIIEVVQ QIKTLRRQVN SRESERAERA
TLVTQERLQL ASSKFKPIKV LDLWIRPPFG GRGRKLTGSL EAHTNGFRYS TSRPDERVDV
LFGNIKHAFF QPAEREMITL VHFHLHNHIM VGNKKTKDVQ FYVEVMDVVQ TLGGGKRSAY
DPDEIEEEQR ERDRKNKINM DFQNFVNRVN DLWGQPQFKA LDLEFDQPMR ELGFHGVPHK
ASAFIVPTSN CLVELIETPF VVISLNEIEI VNLERVGLGQ KNFDMTIVFK DFKRDVLRID
SIPSTSLDGI KEWLNTTDLK YYESRLNLNW RPILKTITDD PEKFIEDGGW EFLNMEVSDS
ESEHSEESDQ GYVPSDVQSD SVSEDEDDDS ESLVESEDDE DEDSDEDSEE DEGKTWEELE
REASYADREK GHDSDSEEER KRRKMKALGK GRVPDKRNPG GSLPKRPKMR
//
