ID A0A0V1L7K6_9BILA Unreviewed; 722 AA.
AC A0A0V1L7K6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=FACT complex subunit SSRP1 {ECO:0000256|RuleBase:RU364013};
GN Name=Ssrp1 {ECO:0000313|EMBL:KRZ54974.1};
GN ORFNames=T02_4568 {ECO:0000313|EMBL:KRZ54974.1};
OS Trichinella nativa.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ54974.1, ECO:0000313|Proteomes:UP000054721};
RN [1] {ECO:0000313|EMBL:KRZ54974.1, ECO:0000313|Proteomes:UP000054721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS10 {ECO:0000313|EMBL:KRZ54974.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (MAY-2015) 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}.
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:KRZ54974.1}.
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DR EMBL; JYDW01000126; KRZ54974.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1L7K6; -.
DR STRING; 6335.A0A0V1L7K6; -.
DR Proteomes; UP000054721; 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; 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:UP000054721};
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 608..672
FT /note="HMG box"
FT /evidence="ECO:0000259|PROSITE:PS50118"
FT DNA_BIND 608..672
FT /note="HMG box"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT REGION 471..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 675..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..578
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..607
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..694
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..714
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 722 AA; 81756 MW; 89E6C3A993949435 CRC64;
MVSLFETTYF GCITMNDFQL EFNDVCMENL GYLNPGKIKL SNQSITFKNT KTGKVEHISA
NDIDHCHWVR LADSPALKCL LKSGPMYRFG GFKDSDFDRL SAYLKKNWNM ELKNIEPCIT
GTNQATANFI GSVLEFENEG QLLFDIPLAN VNNCSSAKNE VIMEFNQNDE CAVSLMEMRL
YISADPNTEE DPAKEFKRKI AEKAGFLKES GKELAVLEQV LCATPRGRYD IKIYPTMLAL
HGKTFDYKIP ISSILRLFLL PHQDGRRMFF VIGLDPPVKQ GQTRYHFLIM DILKDDEIDL
ELGLPEDVLK EKYNGELPRQ LSGPLFEIIS RIMKCLVRKQ ITVPGNFVGH TGTPAVGCAY
KSAGGFLYPL QHGFLYVHKP PVYVRLEEIS CINFARSHVT TKSFDFEIQT KQGNIFTFTS
IMKEEYGKLY DFVVSKGINI TNTGKRLETT ESLFKGSSDE EGERDHYAEH LKSEAREKEE
NNENDSDESD DSDYDPEKGE VRKNSSESSS SSSDSEASGG SEDESSDQEE KNKQKTKNVS
KKAKSSSSAE SDEEKDDGDS DDDDDDDDQE EEEEEEYDDE KPKPKKAHNK KAVQPPKPKK
QKKVKEAPKR NKSAYMFYLM ENQSKFKKPG MSFANVTKVA AEHFKKLKDK SKWENLAAVD
RKRYLNELKE FKKKGGGNIV ATKSSKSSTP VKASKIKSRE IIEDSDSSSD EKMDTTEDSS
DE
//