ID A0A026X2Y7_OOCBI Unreviewed; 1132 AA.
AC A0A026X2Y7;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=FACT complex subunit {ECO:0000256|RuleBase:RU367052};
GN ORFNames=X777_10232 {ECO:0000313|EMBL:EZA62602.1};
OS Ooceraea biroi (Clonal raider ant) (Cerapachys biroi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Dorylinae; Ooceraea.
OX NCBI_TaxID=2015173 {ECO:0000313|EMBL:EZA62602.1, ECO:0000313|Proteomes:UP000053097};
RN [1] {ECO:0000313|EMBL:EZA62602.1, ECO:0000313|Proteomes:UP000053097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24508170; DOI=10.1016/j.cub.2014.01.018;
RA Oxley P.R., Ji L., Fetter-Pruneda I., McKenzie S.K., Li C., Hu H.,
RA Zhang G., Kronauer D.J.;
RT "The genome of the clonal raider ant Cerapachys biroi.";
RL Curr. Biol. 24:451-458(2014).
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; KK107020; EZA62602.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A026X2Y7; -.
DR STRING; 2015173.A0A026X2Y7; -.
DR EnsemblMetazoa; XM_011335157.3; XP_011333459.1; LOC105277033.
DR OMA; YHINTIP; -.
DR OrthoDB; 169847at2759; -.
DR Proteomes; UP000053097; 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:UP000053097};
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..171
FT /note="FACT complex subunit Spt16 N-terminal lobe"
FT /evidence="ECO:0000259|SMART:SM01285"
FT DOMAIN 536..696
FT /note="FACT complex subunit Spt16"
FT /evidence="ECO:0000259|SMART:SM01286"
FT DOMAIN 813..903
FT /note="Histone chaperone RTT106/FACT complex subunit SPT16-
FT like middle"
FT /evidence="ECO:0000259|SMART:SM01287"
FT REGION 439..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 925..1132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..485
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 935..988
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 989..1044
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1054..1074
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1084..1099
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1100..1125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1132 AA; 128815 MW; 7FC34F0D75DC70DC CRC64;
MANVTLDKDM FFRRMKRLYA AWRDGEVGTD DSFSKMDCLI SAVGTDEDIV YSKSTALQTW
LLSYELTDTI MILTEESINF LASKKKIEFL RKVENQKTED TEVPPVKLFV RDRSDEDKAN
FAKLIEVIKQ SKKGKTLGVF SKENYPGAFM DAWRAALKNE SFDTIDISAA TAYIMSPKED
SEILTIKKAC LVSVDVFTKY LKDQIMEIID SDKKVKHSKL AEGVDTAITN KKYVTGVDIS
QVDMCYPAII QSGGNYSLKF SAVSDKNTTL HFGVIICSLG ARYKSYCSNI VRTLLVNPTK
MIEENYNFLL QLEEEILKKL VAGAKISEVY EAGIKFVKDE KPEMQNHLTK NFGFAMGIEF
KESSLLLGPK THATLKKGMV YNVNVGLANL TNPDATDKEG KMYALFVGDT VIVNEGQPAT
NLTPSKKKVK NIGIYVKDDE DDEEEGSGKE NERKPEILGR GKRTAVIESK LRTEHSSEEK
RKQHQKELAQ QLNKIAKARL AQQSGGKEQE KIRKSTVSYK SLNHMPREPE VKELKLYVDK
KYETVILPVS GIPVPFHIST IKNISQSVEG DYTYLRINFF HPGATMGRNE GGSYPQPDAT
FVKEVTYRST NTKEPGEISA PSSNLNTAFR LIKEVQKKFK NREAEEREKE DLVKQDTLIL
SQNKGNPKLK DLYIRPNIVT KRMTGGLEAH TNGFRYTSVR GDKVDILYNN IKNAFFQPCD
GEMIILLHFH LKHAIMFGKK KHVDVQFYTE VGEITTDLGK HQHMHDRDDL AAEQSERELR
HKLKTAFKSF CEKVEGMTKQ EIEFDTPFRD LGFPGAPYRS TVLLQPTSGC LVNLTEWPPF
VITLEDVELV HFERVQFHLK NFDMIFVFKD YHRKVAMVNA IPMNMLDHVK EWLNSCDIRY
SEGVQSLNWT KIMKTITDDP EGFFDSGGWT FLDPESDAEN EEVEDEEEEE DDAYEPTDIE
SEEESDDDSE YSEASEDSDS EEEELGSSEE SGKDWSDLER EAAEEDKERG EDRYHDDYSS
NKKKKSTRRQ TLSPSKDRHN SKHKSSTSSK SKSSSSSKDK RSSDKHRTDR SRSGGSNKRG
SPSKSSKHSP KKSNKHDKRE KSKSSHSSSS SKKRSREDSS ERNNRGSKRS KK
//
