ID H0EZ55_GLAL7 Unreviewed; 1061 AA.
AC H0EZ55;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Replication factor C subunit 1 {ECO:0000256|ARBA:ARBA00020401, ECO:0000256|PIRNR:PIRNR036578};
GN ORFNames=M7I_8117 {ECO:0000313|EMBL:EHK96209.1};
OS Glarea lozoyensis (strain ATCC 74030 / MF5533).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Helotiaceae; Glarea.
OX NCBI_TaxID=1104152 {ECO:0000313|EMBL:EHK96209.1, ECO:0000313|Proteomes:UP000005446};
RN [1] {ECO:0000313|EMBL:EHK96209.1, ECO:0000313|Proteomes:UP000005446}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 74030 / MF5533 {ECO:0000313|Proteomes:UP000005446};
RX PubMed=22302591; DOI=10.1128/EC.05302-11;
RA Youssar L., Gruening B.A., Erxleben A., Guenther S., Huettel W.;
RT "Genome sequence of the fungus Glarea lozoyensis: the first genome sequence
RT of a species from the Helotiaceae family.";
RL Eukaryot. Cell 11:250-250(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}.
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:EHK96209.1}.
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DR EMBL; AGUE01000270; EHK96209.1; -; Genomic_DNA.
DR AlphaFoldDB; H0EZ55; -.
DR HOGENOM; CLU_003574_1_1_1; -.
DR InParanoid; H0EZ55; -.
DR Proteomes; UP000005446; 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; cd17752; BRCT_RFC1; 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:SF6; 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:UP000005446}.
FT DOMAIN 317..396
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 1..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 963..1061
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..74
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..236
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..449
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 977..997
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 998..1014
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1061 AA; 117110 MW; F12661A13254265F CRC64;
MPADIRNFFG NKTSTPIREK EVKKEEDPKK KRAKSRKIID DSDEEEPVPK KATPKKAPPK
KPTKKEEPKA EETTTEDYFA STSKSKPKST KSTPRKPNPP PNTETSSRSS TRKAKAVVYN
NNLADEELAF LDDDEDAGDD IFAAGVKKAG KEKDAYVESE SDDEPVVAKQ NKPSANRKAS
RTDGDVSGKT ATAERHASPD VIMIDQPTGS VTSRKRKSVE LDSEEDEEEI KPKIKSVKSQ
STKPPPAKKA RAPAKKPLET EKSAVQAILD NIPTVRAPTP PAKDPNHKYD WKKGGQGGGG
GNAGPPPAAG SKEMPVGAEN CLAGMSFVFT GLLETLSRDD GQALVKRYGG KVTTAPSGKT
SFVVLGSDAG PSKLRKIHEL KIKTIDEDGL FSIIRELPAN GGDGQAAEKH MEKKTAEMEK
IKREAEEMEK EERKKALEAE KDRKTAEKLA AATGSRAPPP RAPPPSSLLW TSKYAPTAIN
QICGNKGQVE KIQKWLKGWA QAHKYEFSKK GPDGLGGYRA IMIHGPPGIG KTTAAHLAAK
LAGYDVLENN ASDTRSKKMV ETGLNEVLSN NSLRGYYAGD GKPVDATKKN IVLIMDEVDG
MSAGDRGGVG AMAKICKKTD IPMILICNEF NQQKMKPFEH VTFPIPFKRP TVDMVRSRIA
TICHREGMKL PMNVIDALIE GSNKDIRQII NMISTAKLDE SSMDFDDTKA MTKAWEKSVV
LKPWDICHKI LGGGMFAPSS KATLNDKLEL YFNDHEKSFL MVQENYLNQK PMLASSYQGR
QQHLKTLQLM DQAAESISDG DLVDRMIHGS QQQWSLMPTH GIFSMVRPAS FISGAGSGTK
FTTWLGNNSK QGKLTRYVKE IQSHMRLRTS GDRHEIRQQY LPVLWTRLID RLQREGKSAA
EEVIELMDSY FLTREDFDFI MELGLGPQDE SRVKIDSQAK ATFTRLYNQK SHPMPFMKAS
NVMAPAAKSK ADKPDLEEAL EEDDEPEAAE PEVKAEDEIL EEELKKDKFI KQPKSKKPAA
KKPAKKKASK AEEDDEEDSE EEVKPKPKAK AKATSKGKSK K
//
