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Database: UniProt
Entry: D8U9V6_VOLCA
LinkDB: D8U9V6_VOLCA
Original site: D8U9V6_VOLCA 
ID   D8U9V6_VOLCA            Unreviewed;       645 AA.
AC   D8U9V6;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   24-JAN-2024, entry version 57.
DE   RecName: Full=FACT complex subunit SSRP1 {ECO:0000256|RuleBase:RU364013};
GN   ORFNames=VOLCADRAFT_76727 {ECO:0000313|EMBL:EFJ43539.1};
OS   Volvox carteri f. nagariensis.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Volvocaceae; Volvox.
OX   NCBI_TaxID=3068 {ECO:0000313|Proteomes:UP000001058};
RN   [1] {ECO:0000313|EMBL:EFJ43539.1, ECO:0000313|Proteomes:UP000001058}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=f. Nagariensis / Eve {ECO:0000313|Proteomes:UP000001058};
RX   PubMed=20616280; DOI=10.1126/science.1188800;
RA   Prochnik S.E., Umen J., Nedelcu A.M., Hallmann A., Miller S.M., Nishii I.,
RA   Ferris P., Kuo A., Mitros T., Fritz-Laylin L.K., Hellsten U., Chapman J.,
RA   Simakov O., Rensing S.A., Terry A., Pangilinan J., Kapitonov V., Jurka J.,
RA   Salamov A., Shapiro H., Schmutz J., Grimwood J., Lindquist E., Lucas S.,
RA   Grigoriev I.V., Schmitt R., Kirk D., Rokhsar D.S.;
RT   "Genomic analysis of organismal complexity in the multicellular green alga
RT   Volvox carteri.";
RL   Science 329:223-226(2010).
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   -!- SUBUNIT: Component of the FACT complex, a stable heterodimer of SPT16
CC       and SSRP1. {ECO:0000256|ARBA:ARBA00011111}.
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; GL378372; EFJ43539.1; -; Genomic_DNA.
DR   RefSeq; XP_002955468.1; XM_002955422.1.
DR   AlphaFoldDB; D8U9V6; -.
DR   STRING; 3068.D8U9V6; -.
DR   GeneID; 9616740; -.
DR   KEGG; vcn:VOLCADRAFT_76727; -.
DR   eggNOG; KOG0526; Eukaryota.
DR   InParanoid; D8U9V6; -.
DR   OrthoDB; 5488575at2759; -.
DR   Proteomes; UP000001058; Unassembled WGS sequence.
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; cd01390; HMG-box_NHP6-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:UP000001058};
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          555..623
FT                   /note="HMG box"
FT                   /evidence="ECO:0000259|PROSITE:PS50118"
FT   DNA_BIND        555..623
FT                   /note="HMG box"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT   REGION          452..562
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          623..645
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        462..482
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        483..517
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        518..554
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   645 AA;  69944 MW;  A6DF6EFF471366AA CRC64;
     MAEGVQAFGE IWLGSRGGVS SGQLKLTPAG FVWRRKQGGK NVEVKKEEVE GLSWTKVPRG
     CQLSVRRKGA TTLNFLGFRD KDLDALQHYA RNALDHPEGI SEEALSTSGH NWGAVQLRGA
     SLAFMVGSKV AFELPLADVC TAQQMKDDVM LELHVDDTGG EVAEDMLQEL AFYVPPGNEE
     FPARGEDVPA SKALLDALLP HADTEAAAAD EPVCVFSEVG ILAPRGRFDI EMHLGYLQLG
     GQSQDFKVRY TSIQRIFILP KQNTPHTLVV ISLDPPIRKG QTYYAHLLCQ FPTEDDITVE
     LDISEEALVS KNEKNGGKLS SEMSGPVHEV FAKLLRGLSG ARITKPGHFR NAAGDGFSVR
     CSYKADDGQL YPLDRGFFYV HKPPLLIPDN DIESVEFARQ GSGAVSSSVR TFDLVIRLKG
     GTEHMFRNIQ RSEWGNLFEF INTKKIPIEN LASAKRGPGG AHAGVDAEDD MDPGMRRAAA
     EADYDEDDED EDFDASGGSE SSEDEDEDGE SDAEMIEEED GKGAAKGKGK GAAKADGAEG
     AKPKKERKPK DPNAPKKNLT GFMYFSNANR EKVKAENPGI AFGEIGKMLG ERWKGMGADE
     KAPYEQMAAK DKVRYAEAMK AYKERGGAAA GGKDGDGSDA GGDDE
//
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