ID A8NEJ9_COPC7 Unreviewed; 604 AA.
AC A8NEJ9;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Replication protein A subunit {ECO:0000256|RuleBase:RU364130};
GN ORFNames=CC1G_01113 {ECO:0000313|EMBL:EAU88740.1};
OS Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS (Inky cap fungus) (Hormographiella aspergillata).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Psathyrellaceae; Coprinopsis.
OX NCBI_TaxID=240176 {ECO:0000313|EMBL:EAU88740.1, ECO:0000313|Proteomes:UP000001861};
RN [1] {ECO:0000313|EMBL:EAU88740.1, ECO:0000313|Proteomes:UP000001861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003
RC {ECO:0000313|Proteomes:UP000001861};
RX PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA Burns C., Canback B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA Kues U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.J.,
RA Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA Zolan M.E., Pukkila P.J.;
RT "Insights into evolution of multicellular fungi from the assembled
RT chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
CC -!- FUNCTION: As part of the replication protein A (RPA/RP-A), a single-
CC stranded DNA-binding heterotrimeric complex, may play an essential role
CC in DNA replication, recombination and repair. Binds and stabilizes
CC single-stranded DNA intermediates, preventing complementary DNA
CC reannealing and recruiting different proteins involved in DNA
CC metabolism. {ECO:0000256|RuleBase:RU364130}.
CC -!- SUBUNIT: Component of the heterotrimeric canonical replication protein
CC A complex (RPA). {ECO:0000256|RuleBase:RU364130}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU364130}.
CC -!- SIMILARITY: Belongs to the replication factor A protein 1 family.
CC {ECO:0000256|ARBA:ARBA00005690, ECO:0000256|RuleBase:RU364130}.
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:EAU88740.1}.
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DR EMBL; AACS02000002; EAU88740.1; -; Genomic_DNA.
DR RefSeq; XP_001833051.1; XM_001832999.1.
DR AlphaFoldDB; A8NEJ9; -.
DR STRING; 240176.A8NEJ9; -.
DR GeneID; 6009542; -.
DR KEGG; cci:CC1G_01113; -.
DR VEuPathDB; FungiDB:CC1G_01113; -.
DR eggNOG; KOG0851; Eukaryota.
DR InParanoid; A8NEJ9; -.
DR OMA; FNDQCDA; -.
DR OrthoDB; 1122034at2759; -.
DR Proteomes; UP000001861; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd04474; RPA1_DBD_A; 1.
DR CDD; cd04475; RPA1_DBD_B; 1.
DR CDD; cd04476; RPA1_DBD_C; 1.
DR CDD; cd04477; RPA1N; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 4.
DR InterPro; IPR047192; Euk_RPA1_DBD_C.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR InterPro; IPR013955; Rep_factor-A_C.
DR InterPro; IPR007199; Rep_factor-A_N.
DR InterPro; IPR031657; REPA_OB_2.
DR InterPro; IPR004591; Rfa1.
DR NCBIfam; TIGR00617; rpa1; 1.
DR PANTHER; PTHR23273; REPLICATION FACTOR A 1, RFA1; 1.
DR PANTHER; PTHR23273:SF4; REPLICATION PROTEIN A 70 KDA DNA-BINDING SUBUNIT; 1.
DR Pfam; PF04057; Rep-A_N; 1.
DR Pfam; PF08646; Rep_fac-A_C; 1.
DR Pfam; PF16900; REPA_OB_2; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 4.
PE 3: Inferred from homology;
KW DNA replication {ECO:0000256|RuleBase:RU364130};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU364130};
KW Metal-binding {ECO:0000256|RuleBase:RU364130};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU364130};
KW Reference proteome {ECO:0000313|Proteomes:UP000001861};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU364130};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|RuleBase:RU364130}.
FT DOMAIN 30..114
FT /note="Replication factor-A protein 1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04057"
FT DOMAIN 184..264
FT /note="OB"
FT /evidence="ECO:0000259|Pfam:PF01336"
FT DOMAIN 293..389
FT /note="Replication protein A OB"
FT /evidence="ECO:0000259|Pfam:PF16900"
FT DOMAIN 450..593
FT /note="Replication factor A C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08646"
FT REGION 119..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 604 AA; 67312 MW; 865C5F4F363C5E1B CRC64;
MSTTDVQLTA GSCERLQFAN PQDASVFESP HTIQFLSIKK VNTANPNSNA PVDRYRIIIS
DGVHFIQAML ATQLNELVQN NSIGKHTVAV VERATCNYVQ EKRLIVVLEL RVVAHLPDKI
GDPQQLGPDS KRALDSASVT PAPQSVATSG PSTSTKTAPA KPATTGPQRG VYPIEGLSPY
QNNWTIKARV TQKSEMKQWS NAQGEGKLFN VTFMDDSGEI RATAFNLVAD DLYPKLEEGK
VYYVSKARVG LAKKKFSNIP NDYELSLERN TEIEECHETT NLPTIKYNFV PLNGLDALAK
DAICDVIGVV KDVGEVGTIT SRSNNRQISK RDLTLVDKSA YSVRMTLWGK QAEQFKVEPE
SIIAFKGVRV GDFNGRNLSM TSASTMQVNP DIEECFTLRG WYDSQGQTQT FQAQSSNNLG
GTSLGFRRDE ARTLEDVKQA GFGQSDKPDY FSTRATIIHI KDDNIAYPAC PTQGCNKKVI
EEADGWRCEK CEKVFEAPEY RYIMSMMVAD HTGKAWFQGF NEVGVTVYGM SANDLVQIKN
NDHAQYKAIQ YHAACNTYNF SCRAKEDEFN GVRRVRFGIS RLAKVDYKEE AGYLRDLLYS
SWAR
//
