ID A0A026W7R0_OOCBI Unreviewed; 732 AA.
AC A0A026W7R0;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=FACT complex subunit SSRP1 {ECO:0000256|RuleBase:RU364013};
GN ORFNames=DMN91_009702 {ECO:0000313|EMBL:RLU17467.1}, X777_09059
GN {ECO:0000313|EMBL:EZA52038.1};
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:EZA52038.1, ECO:0000313|Proteomes:UP000053097};
RN [1] {ECO:0000313|EMBL:EZA52038.1, 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).
RN [2] {ECO:0000313|EMBL:RLU17467.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Clonal line C1 {ECO:0000313|EMBL:RLU17467.1};
RX PubMed=30249741; DOI=10.1101/gr.237123.118;
RA McKenzie S.K., Kronauer D.J.C.;
RT "The genomic architecture and molecular evolution of ant odorant
RT receptors.";
RL Genome Res. 28:1757-1765(2018).
RN [3] {ECO:0000313|EMBL:RLU17467.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Clonal line C1 {ECO:0000313|EMBL:RLU17467.1};
RA Mckenzie S.K., Kronauer D.J.C.;
RL Submitted (JUL-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:RU364013}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU364013}.
CC Chromosome {ECO:0000256|RuleBase:RU364013}.
CC -!- SIMILARITY: Belongs to the SSRP1 family.
CC {ECO:0000256|ARBA:ARBA00010060, ECO:0000256|RuleBase:RU364013}.
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DR EMBL; KK107356; EZA52038.1; -; Genomic_DNA.
DR EMBL; QOIP01000010; RLU17467.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A026W7R0; -.
DR STRING; 2015173.A0A026W7R0; -.
DR EnsemblMetazoa; XM_011344159.3; XP_011342461.2; LOC105282289.
DR OMA; KQPGKCK; -.
DR Proteomes; UP000053097; Unassembled WGS sequence.
DR Proteomes; UP000279307; Chromosome 10.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd21994; HMG-box_SSRP1-like; 1.
DR CDD; cd13230; PH1_SSRP1-like; 1.
DR CDD; cd13231; PH2_SSRP1-like; 1.
DR Gene3D; 2.30.29.150; -; 1.
DR Gene3D; 1.10.30.10; High mobility group box domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2.
DR Gene3D; 2.30.29.220; Structure-specific recognition protein (SSRP1); 1.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR013719; RTT106/SPT16-like_middle_dom.
DR InterPro; IPR048993; SSRP1-like_PH1.
DR InterPro; IPR000969; SSRP1/POB3.
DR InterPro; IPR035417; SSRP1/POB3_N.
DR InterPro; IPR024954; SSRP1_DD.
DR InterPro; IPR038167; SSRP1_sf.
DR PANTHER; PTHR45849; FACT COMPLEX SUBUNIT SSRP1; 1.
DR PANTHER; PTHR45849:SF1; FACT COMPLEX SUBUNIT SSRP1; 1.
DR Pfam; PF00505; HMG_box; 1.
DR Pfam; PF21103; PH1_SSRP1-like; 1.
DR Pfam; PF17292; POB3_N; 1.
DR Pfam; PF08512; Rttp106-like_middle; 1.
DR Pfam; PF03531; SSrecog; 1.
DR PRINTS; PR00887; SSRCOGNITION.
DR SMART; SM00398; HMG; 1.
DR SMART; SM01287; Rtt106; 1.
DR SUPFAM; SSF47095; HMG-box; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50118; HMG_BOX_2; 1.
PE 3: Inferred from homology;
KW Chromosome {ECO:0000256|ARBA:ARBA00022454, ECO:0000256|RuleBase:RU364013};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU364013};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU364013};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW ECO:0000256|RuleBase:RU364013};
KW DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00267};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00267}; Reference proteome {ECO:0000313|Proteomes:UP000053097};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU364013};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW ECO:0000256|RuleBase:RU364013}.
FT DOMAIN 551..617
FT /note="HMG box"
FT /evidence="ECO:0000259|PROSITE:PS50118"
FT DNA_BIND 551..617
FT /note="HMG box"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT REGION 458..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 615..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..502
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..527
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..548
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..643
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..690
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..712
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 732 AA; 83305 MW; 1C1B3268BDFC57FB CRC64;
MDFLEYPDIF AEVKGAMTPG RLKLTDQHLI FKNQKTGKVE QISASDMEMV NYQKFIGTWG
LRIFLKNGTL HRFKGFKEAD QEKIAKFFSI NYKKDMLEKE LSLKGWNWGT AKFSGSILSF
DVGHHTAFEI PLYDVSQCNT GKNEVTLEFH QNDDAPVSLM EMRFHIPVSD SVDQDPVEAF
HQQVMEKASV ISVSGDAIAI FREIHCLTPR GRYDIKIFQS FFQLHGKTFD YKIPMSTVLR
LFLLPHKDNR QMFFVVSLDP PIKQGQTRYH YLVLLFNQEE ETSIELPFTE KELKEKYEDK
LTKELSGPTY EVLGKVMKVI INRKLTGPGH FTGHTGTPAI GCSFKAAAGY LYPLERGFIY
VHKPPIHIRF EEIASVNFAR GGGSTRSFDF EIELTSGVVH TFSSIEKEEY GKLFDFITSK
KLRVKNRGKS DKLNYDEDFG DSDQEDEPDA YLARVKAEAQ ERDGDENQDS EDASSDEEFK
PNQDESDVAE EYDTDANSSE SDEDSDASAA SHKKEKKEKE KEKKKPKTAK TAPKKTRKSR
KPKKQKDANR PKRPPTAFML WLNSTRESIK ADNPGIAVTE IAKKGGEMWR ELKDKSEWEA
KAAKAKKEYA ASIKEYEASG GGKAKEKKEK TEKKKKETKK DSPSKMMTGT AFKSKEYISD
DDSSSDESKK SEKKQSQNNE SEEEKRKKKK RPVESSGKKT TKKAKRESDE SDAEEPVEST
PPSSDAESKD SD
//
