ID K5XG25_AGABU Unreviewed; 913 AA.
AC K5XG25;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Replication factor C subunit 1 {ECO:0000256|ARBA:ARBA00020401, ECO:0000256|PIRNR:PIRNR036578};
GN ORFNames=AGABI1DRAFT_119115 {ECO:0000313|EMBL:EKM82182.1};
OS Agaricus bisporus var. burnettii (strain JB137-S8 / ATCC MYA-4627 / FGSC
OS 10392) (White button mushroom).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Agaricaceae; Agaricus.
OX NCBI_TaxID=597362 {ECO:0000313|EMBL:EKM82182.1, ECO:0000313|Proteomes:UP000008493};
RN [1] {ECO:0000313|Proteomes:UP000008493}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JB137-S8 / ATCC MYA-4627 / FGSC 10392
RC {ECO:0000313|Proteomes:UP000008493};
RX PubMed=23045686; DOI=10.1073/pnas.1206847109;
RA Morin E., Kohler A., Baker A.R., Foulongne-Oriol M., Lombard V., Nagy L.G.,
RA Ohm R.A., Patyshakuliyeva A., Brun A., Aerts A.L., Bailey A.M.,
RA Billette C., Coutinho P.M., Deakin G., Doddapaneni H., Floudas D.,
RA Grimwood J., Hilden K., Kuees U., LaButti K.M., Lapidus A., Lindquist E.A.,
RA Lucas S.M., Murat C., Riley R.W., Salamov A.A., Schmutz J., Subramanian V.,
RA Woesten H.A.B., Xu J., Eastwood D.C., Foster G.D., Sonnenberg A.S.,
RA Cullen D., de Vries R.P., Lundell T., Hibbett D.S., Henrissat B.,
RA Burton K.S., Kerrigan R.W., Challen M.P., Grigoriev I.V., Martin F.;
RT "Genome sequence of the button mushroom Agaricus bisporus reveals
RT mechanisms governing adaptation to a humic-rich ecological niche.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:17501-17506(2012).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR036578}.
CC -!- SIMILARITY: Belongs to the activator 1 large subunit family.
CC {ECO:0000256|ARBA:ARBA00006116, ECO:0000256|PIRNR:PIRNR036578}.
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DR EMBL; JH971387; EKM82182.1; -; Genomic_DNA.
DR RefSeq; XP_007327896.1; XM_007327834.1.
DR AlphaFoldDB; K5XG25; -.
DR STRING; 597362.K5XG25; -.
DR GeneID; 18825530; -.
DR KEGG; abp:AGABI1DRAFT119115; -.
DR eggNOG; KOG1968; Eukaryota.
DR HOGENOM; CLU_003574_1_0_1; -.
DR InParanoid; K5XG25; -.
DR OMA; LICNERN; -.
DR OrthoDB; 6297at2759; -.
DR Proteomes; UP000008493; Unassembled WGS sequence.
DR GO; GO:0005663; C:DNA replication factor C complex; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003689; F:DNA clamp loader activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0006271; P:DNA strand elongation involved in DNA replication; IEA:UniProt.
DR CDD; cd00009; AAA; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.20.272.10; -; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR InterPro; IPR013725; DNA_replication_fac_RFC1_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR012178; RFC1.
DR PANTHER; PTHR23389; CHROMOSOME TRANSMISSION FIDELITY FACTOR 18; 1.
DR PANTHER; PTHR23389:SF37; REPLICATION FACTOR C SUBUNIT 1; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF08519; RFC1; 1.
DR PIRSF; PIRSF036578; RFC1; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00292; BRCT; 1.
DR SUPFAM; SSF52113; BRCT domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF48019; post-AAA+ oligomerization domain-like; 1.
DR PROSITE; PS50172; BRCT; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PIRNR:PIRNR036578};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW ECO:0000256|PIRNR:PIRNR036578};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR036578};
KW Nucleus {ECO:0000256|PIRNR:PIRNR036578};
KW Reference proteome {ECO:0000313|Proteomes:UP000008493}.
FT DOMAIN 215..296
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 1..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 828..913
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 304..331
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 20..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..98
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..168
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 859..874
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 875..891
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 895..913
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 913 AA; 99711 MW; EB849F3D102597B4 CRC64;
MAPKTNKSGK GGGKDIRTFF GGSQKSSGSG SAAYLTGCRS SKPINTDSDD EPIGPSKLTG
RMVLDGSEDE NPRPPQKRKA PLRVDDDESR EDSPPRKKAS ISSTKANVRK SVKPRKDEDY
EIEKSSSEED FIDDEPDDIK TKVKRKSSSS KKEKATKSEP ENKKVAPTKA AAKPKSANLH
LHRSLITNIF DSWAAIKAAK LAGPSAPGSK QVPDGAPNCL LGLSFVFTGE LSSFSREEAV
DLAKRFGGRV VLQPSSKTDF VVLGDDAGPA KLAAIKKHGL KTLSEDEFLN LIATREGADE
GGLDAKTKKK LEKEQQEIRK AAKEMEKREN SSSHVQLDPS IQLWTTRYAP QSLKEICGNK
GQVEKLLQWL NDWPSSLKSG FKKPGKIGMN IFRGVLITGP PGIGKTTSAH LCAKLAGFTP
IELNASDTRS KKLVENGMNI NNTSLDGFIH GAGSTNSVGV PITGKTCLIM DEVDGMSAGD
RGGVGALNAI IKKSKIPIIC IANDRGAQKL KPLMSTTFSL NFSRWDSNTH RKLVLTNAPD
QGMKVPANVV DQLIQGSQSD IRQVLNMLST WKLSSDSMDF DESKSLVKMN EKYAIMTPFD
ITSKILGPYL FSSTARETLG DKMELYFQDH SFVPLFIQEN YLKSQPARVR NLDGPEKELK
HLQLMEQASA SISDGDLVDS LIHGPEQHWG LMPLHAVCST VRPASCLYGS GVHFGGPNSM
SFPQWLGQNS KKNKLARQLA DVQVRMRLKV SSDKAEIRQS YVPALFPYIV RPLVDEGAGA
VDKVIERMDA YYLSKEDWET IVELGVGENK DVKIASAAKS SFTRKYNGSD HPIPFHKAQD
LGKMPKKLTG GPAPDLEEAF IDDIPDDEEE DVKPKESIDD ISGDKLIQAP KKRKAVGTTK
AKTKTKTKTS KKS
//
