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Database: UniProt
Entry: A0A1Q2YJV1_9ASCO
LinkDB: A0A1Q2YJV1_9ASCO
Original site: A0A1Q2YJV1_9ASCO 
ID   A0A1Q2YJV1_9ASCO        Unreviewed;      1031 AA.
AC   A0A1Q2YJV1;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=FACT complex subunit {ECO:0000256|RuleBase:RU367052};
GN   ORFNames=PMKS-003351 {ECO:0000313|EMBL:GAV29846.1};
OS   Pichia membranifaciens.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Pichiaceae; Pichia.
OX   NCBI_TaxID=4926 {ECO:0000313|EMBL:GAV29846.1, ECO:0000313|Proteomes:UP000186136};
RN   [1] {ECO:0000313|EMBL:GAV29846.1, ECO:0000313|Proteomes:UP000186136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KS47-1 {ECO:0000313|EMBL:GAV29846.1,
RC   ECO:0000313|Proteomes:UP000186136};
RA   Konishi M., Ishida M., Arakawa T., Kato Y., Horiuchi J.;
RT   "Whole genome shotgun sequence of Pichia membranifaciens KS47-1.";
RL   Submitted (AUG-2016) 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:GAV29846.1}.
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DR   EMBL; BDGI01000143; GAV29846.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q2YJV1; -.
DR   Proteomes; UP000186136; 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   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   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:UP000186136};
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          6..169
FT                   /note="FACT complex subunit Spt16 N-terminal lobe"
FT                   /evidence="ECO:0000259|SMART:SM01285"
FT   DOMAIN          570..719
FT                   /note="FACT complex subunit Spt16"
FT                   /evidence="ECO:0000259|SMART:SM01286"
FT   DOMAIN          841..931
FT                   /note="Histone chaperone RTT106/FACT complex subunit SPT16-
FT                   like middle"
FT                   /evidence="ECO:0000259|SMART:SM01287"
FT   REGION          448..546
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          957..1031
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        448..468
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        469..491
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        519..546
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        964..1031
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1031 AA;  118405 MW;  94342CBF818DA2E8 CRC64;
     MSDIAIDPAL FRRRLHLIQK NIFSNESFQK VNGLLIIVGS SDDSNPYQKS TVMHTWLLGY
     EFPATAIYIT NKKIYFVTSV SKAKYLQPLV NSPNSNNNIV IFSRNKDPEH NKNQFEKFFK
     EVENTISESN NSIGVLSKDK YQGKFISEWN PLWDEHKTKF ELKDVSLGVS ETLEFKDEEE
     QRNLRTAART SVNMMSYFTD EMSKIVDEDL NVSNSKLVDK VENKIDDAKF FKSIETNKAM
     KKLGKDFDLN NLDWCYKPII QSNGKYELKF SVESTNDKLS GPVIMASLGL RYSNYCSSLS
     RTFLIAPSKE MEKNYEFLFS LQEHIFAILK DGAKFSHVYG EAVQFIEQNR PELKDHFMKN
     IGSLIGIDFR DSAGVINAKN DRVFKENSVV NLVLGFSNLK DSEKGQYALL LSDTVRITGS
     EPIILTESPK LKKEIAFYFD ENDNIKEEGE LEANGSKIKS EKTSEPKSSK SSKSSSTKVK
     NESSMKTENF GNTRVLKAKR RSEQNNAEEG QIQIQKEIQS ELHSKRQKEG LERFNPEDAK
     DGSEQRAVFK RYESYVRESQ IPNNVKDLKI HIDSKNQTII LPIMGRPVPF HINSYKNGSK
     IEEGDYTHLR LNFNSPGLMI TKREELPYES GEDKQFIRSL TFRSKDGARM TEVLKRISEM
     KKSAVKRESE KRERADVVSQ ASLIEVNRPK RLDNVFVRPT PDTKRFPGFV TIHQNGIRYQ
     SLTRDQRVDV LFSNIKHLFF QSCKGELLVI IHAHLRTPIM IGKKKTYDVQ LYREATDMSI
     DETGNRKRKY RYGDEDELEQ EQEERRRRAM LDKEFRAFAE AIADTSGGLV DLDIPFRELG
     FQGVPSRSAV VCLPTRDCLV QLVDLPFLVI TLEEVEIAHL ERVQFGLKNF DMVFVFKDFS
     RPVVHISTIP METLEDVKAW LTDVDIPYSE GPVNLNWPTI MKTIQSDPFG FFQDGGWSFL
     GGDGDSEEEA EEETAESDFD PSDEDPQDEE DYSEEEEDEE EEDDDDDDAS VEEDEDDIAD
     SDELSEEAFS D
//
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