ID A0A1Y2EXL8_9BASI Unreviewed; 859 AA.
AC A0A1Y2EXL8;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Replication factor C subunit 1 {ECO:0000256|ARBA:ARBA00020401, ECO:0000256|PIRNR:PIRNR036578};
GN ORFNames=BCR35DRAFT_124552 {ECO:0000313|EMBL:ORY75974.1};
OS Leucosporidium creatinivorum.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Leucosporidiales; Leucosporidium.
OX NCBI_TaxID=106004 {ECO:0000313|EMBL:ORY75974.1, ECO:0000313|Proteomes:UP000193467};
RN [1] {ECO:0000313|EMBL:ORY75974.1, ECO:0000313|Proteomes:UP000193467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=62-1032 {ECO:0000313|EMBL:ORY75974.1,
RC ECO:0000313|Proteomes:UP000193467};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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:ORY75974.1}.
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DR EMBL; MCGR01000036; ORY75974.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2EXL8; -.
DR STRING; 106004.A0A1Y2EXL8; -.
DR InParanoid; A0A1Y2EXL8; -.
DR OrthoDB; 6297at2759; -.
DR Proteomes; UP000193467; 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 CDD; cd18140; HLD_clamp_RFC; 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 InterPro; IPR047854; RFC_lid.
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|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR036578};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW ECO:0000256|PIRNR:PIRNR036578};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR036578}; Nucleus {ECO:0000256|PIRNR:PIRNR036578};
KW Reference proteome {ECO:0000313|Proteomes:UP000193467}.
FT DOMAIN 170..247
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 1..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 816..859
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..61
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 859 AA; 93883 MW; 46D8C4D7E6B9EC47 CRC64;
MSKSKAAEII LSDSDDDTGV APSFKAKPKA STSSVAKKRA PKIEDSDSDA MDVDVKPKKK
SPAKSTTTVA KKRKSKVVDS DATVTSTDEE DVKPKKARVG VAKPGTKPVP KKAKIEDSDD
DEDVKGKGKA KAPPAKKPKV VKDEKPEKPK WTFKAKTGPA NPGSKDIPAG EDNCLAGLTF
VFTGELESLS REAGQDLAKR YGGRVTTAPS SKTSYVVLGT DAGPKKLEMI AKHKIKTLTE
DQFLELIGSR PSGADDPKFI AKQKEEAEKV KKEAKAIGPK KDDAAHKTQL WTVKYAPSKL
SEICGNKGSV EKLERWLTAW PKALKSDFKK PGPDAMGAFR CVLISGPPGI GKTTAAHLIA
KLQGYDVLEL NASDVRSKKL LETAFRSKIS DTTLSGFFKK DGEDANGLGV NRKSIIIMDE
VDGMSAGDRG GVGALNAMIR KTKVPIIAIC NDKSSPKMKP LTATCFNLPF KRPSASEIRS
RMMSVAFKEG IKVDGKVMDQ LVAGSQSDIR QIVNMLSTWK LSAGPMDYDS GKKLAKMNEK
NAIQTPWTLY SKLTAPQAFG NVSGMTLNDK QELYFQDHQI MPLFVQENYI KNKFQRASGL
QGQDLKLKNL ELMANASEAI SDGDLVDRMI HGGEQQWSLM PVHGIFSCVR PAYYTYGPGG
YPTFPAWFGK NSTQTKLQRL LGEIQIHMRL KTSGDRKEIR QSYLPTLFEK LVRPIQERGT
EAVEEVIELM DDYYITKEDW DTLVELGVGE GYEMEPLLKS IATQTKSAFT RKYNAGEHPI
PFYRNAAGKP KKVVGGGGPA PDFEDAFVDD DDHLAEDDAE EEDVDDVAAD KLIKNKIKKP
KKTAPAGKEK APAKGKKAK
//
