ID A0A0N4XD98_NIPBR Unreviewed; 1042 AA.
AC A0A0N4XD98;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=FACT complex subunit {ECO:0000256|RuleBase:RU367052};
GN ORFNames=NBR_LOCUS484 {ECO:0000313|EMBL:VDL63160.1};
OS Nippostrongylus brasiliensis (Rat hookworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Heligmosomidae; Nippostrongylus.
OX NCBI_TaxID=27835 {ECO:0000313|Proteomes:UP000038043, ECO:0000313|WBParaSite:NBR_0000048301-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:NBR_0000048301-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDL63160.1, ECO:0000313|Proteomes:UP000271162}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) 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 ---------------------------------------------------------------------------
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 EMBL; UYSL01000210; VDL63160.1; -; Genomic_DNA.
DR STRING; 27835.A0A0N4XD98; -.
DR WBParaSite; NBR_0000048301-mRNA-1; NBR_0000048301-mRNA-1; NBR_0000048301.
DR OMA; YHINTIP; -.
DR Proteomes; UP000038043; Unplaced.
DR Proteomes; UP000271162; 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:UP000271162};
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 9..167
FT /note="FACT complex subunit Spt16 N-terminal lobe"
FT /evidence="ECO:0000259|SMART:SM01285"
FT DOMAIN 528..687
FT /note="FACT complex subunit Spt16"
FT /evidence="ECO:0000259|SMART:SM01286"
FT DOMAIN 804..894
FT /note="Histone chaperone RTT106/FACT complex subunit SPT16-
FT like middle"
FT /evidence="ECO:0000259|SMART:SM01287"
FT REGION 435..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 914..1042
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..451
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 927..986
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 987..1018
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1019..1042
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1042 AA; 118233 MW; 81F73F4407DBDA65 CRC64;
MPEKKVLTAD KELFLRHATI LYEKWNSGQD GLDAVDGLVV IVGQDEGALQ YSKSKAFQIW
LLNTELMDTL MLFTKKGIYV LASNRKADYF NSVKSNEFVG VVPPVTPIHR DKSDKDAANF
AKLLGYIKDD ANNKVGYFSK DTFDSDFCND WQKAFADVEK VDVSSSFAHI FAVKDEKELE
TCRSSATATV NAWSYARKKF IEAIDQEKKV KHSRLANEID AEIGSMKVQG QLAKNKTIET
CYNPIIMSGG NYSLKWSTES SDKLLHYGVI VTSLGARLEN YCTNITRTLM VEPSKNLEET
YEGLLATQAA IIEALKPGAK LSDVYAVGVK TFREKCPSVA DNLYKKDFGF ATGIEFREGG
LTISPKCDEK VKAGMIFIVS AGAEGLVNAK SKDDAGKTVT IALSDTVLVK DGQNEVLTEK
AKSRLKNSVI RFKEEEEDAK DSNKENTEVL GRGKRSVVLT DQTRNKATNE DKRKEHQKML
AQQLNDAARQ RLAQASGSSE AKKVKKSNVS YKSYEKFPVD SEINKLNIYV DKRHDTIILP
IFGIPVPFHI SMIKNCSQSV EGDFTYLRIN FAHPGSQIGK DQAQFPNPLA TYLKELTYRA
SNVKEHGEVA APSNNLTTAF RLIKEIQKRF RTEEAEEREK EGAVKQDKLI LSTAKANPKL
KDLFVRPNII AKRISGSLEA HINGFRYTSL RGDRIDVLYN NIKHAFFQPC DNEMIILLHF
HLKHPVLWGK KKYKDIQFYT EVGEITTDLG KYHHMQDRDD VQSEQMEREM RRKLNSTFQN
FCDKVVKQTN DQFDFDAPFS ELGFLGVPHR SSCMLKPTSS CLVNLTEWPP FIVTLDEVEL
VHFERVSFQL KNFDMVFIFK DYSRKTQMVQ QIPMSSLDNV KEWLNTSDLR YTEGIQSLNW
PKIMKTITDD PEEFFETGGW NFLGADSDQE DEAEDESESE EAYTPSESES GEDESDEDES
EAEATSEDSD DEGSLDSDES EGKDWSDLEE EAARADKKRD QEDERGGGDR DRDRHRHHDR
DRDRKRHRHS GGKNGPPSKR HK
//