ID A0A0P7ACS9_9HYPO Unreviewed; 1049 AA.
AC A0A0P7ACS9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Replication factor C subunit 1 {ECO:0000256|ARBA:ARBA00020401, ECO:0000256|PIRNR:PIRNR036578};
GN ORFNames=AK830_g11450 {ECO:0000313|EMBL:KPM35118.1};
OS Neonectria ditissima.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Neonectria.
OX NCBI_TaxID=78410 {ECO:0000313|EMBL:KPM35118.1, ECO:0000313|Proteomes:UP000050424};
RN [1] {ECO:0000313|EMBL:KPM35118.1, ECO:0000313|Proteomes:UP000050424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R09/05 {ECO:0000313|EMBL:KPM35118.1,
RC ECO:0000313|Proteomes:UP000050424};
RA Gomez-Cortecero A., Harrison R.J., Armitage A.D.;
RT "Draft genome of a European isolate of the apple canker pathogen Neonectria
RT ditissima.";
RL Submitted (SEP-2015) 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:KPM35118.1}.
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DR EMBL; LKCW01000273; KPM35118.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7ACS9; -.
DR STRING; 78410.A0A0P7ACS9; -.
DR OrthoDB; 6297at2759; -.
DR Proteomes; UP000050424; 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:UP000050424}.
FT DOMAIN 318..397
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 83..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 402..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 964..1049
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..66
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..133
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..169
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..200
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..269
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..428
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 976..994
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1017..1036
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1049 AA; 114445 MW; DE0C8B81F7977558 CRC64;
MADIRSFFAP KGGAAPPKPK AQEPPAKSKR TKGRKVIEDS EDEDEVVEQK KTAAKPAPKK
KSTNDEPKGV AISADDYFAS AKNSKLPTSA TPKKPQIKSE VAVRSSPRAT QPAAKPATKP
AAKPAPKPPA PAKNGTAPAK RKATTSYTQP VDEDADAYMD DGDEDDDDIF TADVKGRSKR
KNDDYASDES EDDVLPKPKR VAGRGRPSSK ATAEDDVKLS KTSLARNKRK SPVDDSEESE
EEAPRKKAAT KPRAPRAKKV DDKPEDAEIQ DILNSVATVR PPTPPPKDPN AKFDWKKTVA
GGGNASAQPQ MSAELPEGED ECLTGLTFVF TGVLQAIGRD EGQALVKRYG GKVTGQPSSK
TSFVVLGDDA GPSKLAKIKS HGIKTIDENG LFDLIRKLPA HGGGGKGAQK AQEKKKADED
KVKKQVAEME AEEKARKIEA EKAAKKAAAS RGTSVAKAAA TPAPVQLLTS KYAPTQLNHI
CGNKAQVEKI QAWLKNWAKA KKYDFQRRGA DGMGGERAII ISGPPGIGKT TAAHLAAKLE
GFDVLESNAS DSRSKRLVEA GVSDVMNNTS LRGYFAGDGK DVDATKKKIV LIMDEVDGMS
GGDRGGVGAL ARFCKKTEVP LILICNERKL PKMKPFDHVA FDIRFNRPTV DQVRSRIMTI
CHREGLRLPP AVVDALIEGS NKDIRQIINM ISTAKLDQSS MSFDQTKAMS KAWEKHVILK
PWDICQKMLA GGLFTPASKS TLNDKIELYF NDHEFSFLMI QENYLRTKPM ALNGKGYSPR
EYNLKALELF DNAAESISDG DLVDRMIHGP QQQWSLMPTH AVFSTVRPSS FIAGQLMGSN
FTSWLGNNSK TGKLGRFIRE IHSHMRLRSS GDHNEIRQQY MPLLWNQTVN RLQREGNESV
SEVIDIMDSY FLTRDDFDAI QELGVGPMDE ELVKIESKTK AAFTRTYNAM SHPIPFMKAS
NVVAPKAPKK DAPDLEEAIE DEDEGDAVEA PEVDEEELDL KKDKYIKQPK AKKATKKSKA
AAADDDDDEK PKKGRAKAKA TGAKGKAKK
//
