ID A0A4V1XD45_9PEZI Unreviewed; 1052 AA.
AC A0A4V1XD45;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=Replication factor C subunit 1 {ECO:0000256|ARBA:ARBA00020401, ECO:0000256|PIRNR:PIRNR036578};
GN ORFNames=DL767_011538 {ECO:0000313|EMBL:RYP11969.1};
OS Monosporascus sp. MG133.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Xylariales incertae sedis; Monosporascus.
OX NCBI_TaxID=2211645 {ECO:0000313|EMBL:RYP11969.1, ECO:0000313|Proteomes:UP000293831};
RN [1] {ECO:0000313|EMBL:RYP11969.1, ECO:0000313|Proteomes:UP000293831}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MG133 {ECO:0000313|EMBL:RYP11969.1,
RC ECO:0000313|Proteomes:UP000293831};
RA Robinson A.J., Natvig D.O.;
RT "Complete Genomes of Monosporascus.";
RL Submitted (JUN-2018) 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:RYP11969.1}.
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DR EMBL; QJNX01000759; RYP11969.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4V1XD45; -.
DR STRING; 2211645.A0A4V1XD45; -.
DR Proteomes; UP000293831; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000293831}.
FT DOMAIN 318..397
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 1..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 961..1052
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 408..442
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 20..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..215
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..248
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..269
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 975..998
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1052 AA; 115941 MW; 8711D93715D642F2 CRC64;
MPDIRSFFGP KGGAAPPKPP PKKAEEEGSK RRTKGRKVVD DSDEEEVVEK KPVTRSTPRK
KAVKTEVQGT ATTASEYFAS NKSNAKPADT SEEAKAQPKP NPEVRASPRN KAASTKTDTA
PARKSGRIPS KGRPSTTFKN HDPDDDDDDA FMDDADGGDD IFAADAKSRN KRKNDGYAEE
ESEEEVLPKP KRIASRNKPT VALDDLDDEP LTSKTAKKSK ATPQTKKRKT PEPELEEEED
EPPSRKKPAA KKPRVPREKK PDKPESTEIQ AILDDIPTVR PPTPPAKDPN AKFDWRKAQA
GGGNSGPPPN PTGELPEGEE DCLAGLTFVF TGQLSTVSRE DAQGLVKRYG GKITGAPSSK
TSYVVLGEDA GPSKLAKIRE HGIKTINEEG LFELIRRLPA GGGTGKGAEK VRQKRKEEEE
KIKKQAAEME QEEKARKAEA EKVAKAAAAR GAAKPAPAGA TPAAQLWTVK YAPTQPSHIC
GNKASVEKIQ NWLKNWPKHK QYDFQKRGAD GMGGARAIIV SGPPGIGKTT AAHLAAKLEG
YDVLETNASD ARSKKLVEAG VSEVMNNTSL HGYFAADGKK VDKEKKKIVL IMDEVDGMSA
GDRGGVGALA KFCKKTEVPL ILICNERKLP KMKPFDFVAF DVKFQRPTIE QIRSRMMTVC
HREGLKLSPQ VLDALIEGSN RDIRQIINML STIKLDQTSM DFSQSKDMSK AWEKSIVLKP
WDICQKMLAG GLFTPASKAT LNDKIELYFN DHEFSYLMIQ ENYLRTKPLA LNGKQYNKRE
QTLKALELFD QAAESISDGD LVDRMIHGPQ QHWSLMPTHA VFSTVRPASF VAGQLMGSNF
TSWLGNNSKY GKLARYVREI HSHMRLKSSG DHNEIRQQYL PVLWTQLIQR LAEEGKESVE
DVIELMDSYY LTREDFDSIK ELGVGPQDEE HVDIETQTKA SFTRLYNSMS HPVPFMKASS
VVAPAKASRD KPDLEEAIED EDEAEAIEAA EPVDEEDDDI GKDKYIKKPK AKPTKKAAGK
KATKAAAAAA ADNDEEEEEK PKARGRPKKV KK
//
