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Database: UniProt
Entry: A0A0N4XD98_NIPBR
LinkDB: A0A0N4XD98_NIPBR
Original site: A0A0N4XD98_NIPBR 
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}.
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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
//
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