ID A0A1J9QY50_9PEZI Unreviewed; 1088 AA.
AC A0A1J9QY50;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Replication factor C subunit 1 {ECO:0000256|ARBA:ARBA00020401, ECO:0000256|PIRNR:PIRNR036578};
GN ORFNames=BKCO1_3100029 {ECO:0000313|EMBL:OJD33297.1};
OS Diplodia corticola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Diplodia.
OX NCBI_TaxID=236234 {ECO:0000313|EMBL:OJD33297.1, ECO:0000313|Proteomes:UP000183809};
RN [1] {ECO:0000313|EMBL:OJD33297.1, ECO:0000313|Proteomes:UP000183809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 112549 {ECO:0000313|EMBL:OJD33297.1,
RC ECO:0000313|Proteomes:UP000183809};
RA Fernandes I., De Jonge R., Van De Peer Y., Devreese B., Alves A.,
RA Esteves A.C.;
RT "Proteomics and genomics reveal pathogen-plant mechanisms compatible with a
RT hemibiotrophic lifestyle of Diplodia corticola.";
RL Submitted (OCT-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:OJD33297.1}.
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DR EMBL; MNUE01000031; OJD33297.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J9QY50; -.
DR STRING; 236234.A0A1J9QY50; -.
DR OrthoDB; 6297at2759; -.
DR Proteomes; UP000183809; 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:UP000183809}.
FT DOMAIN 348..427
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 1..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 456..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1003..1088
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..167
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 480..503
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1015..1035
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1061..1080
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1088 AA; 119461 MW; 9FEF16FB54685487 CRC64;
MPADIRSFFG GKPAAQPAKE ESTSEEAMQA EIYSPRSQAK PAAKKRGRPA RKVVEDSDDE
EEPPKKATPK KPAPKKQAKR EATPEGEATT ASAFFGDKKP ARSAPSKASK AAAKTETPKS
TPKKAKASDK TAVTPTRTSA RKKKPATYSE VKDEDEDFLD DDEDGDDIFT AAFKKKGKHA
DDYEESSEDE PVALPQRQAS GRGQKKLKDE GDFEPEADVD MKDAKPEDDF VVPDDDEEIV
DNKSAKKAKP AAKAGRKRKS AETDDELEAE PPKKARGKKT SPAKKKAKKD EPENAAMKEL
LDSIPTVRPP SPPPKDGDAP KKFNPFKAGA HANSGPAPQS GALDIPEGKP NCLAGMTFVF
TGLLEYLDRE AGQQLVKRYG GKVTSGPSSK TSYVVLGSDA GPSKLQKIKQ FKLKTINEEG
LFALIKKLPA NGGDSKAAAA YEQKQAAEEK KIKEMAEEME REERRKGGAG GAGGGSATAA
ARSAASSQAP GSQTSGSQSA QDNRLWTVKY APTQLTQICG NKTQVEKLQR WLRNFPKSQK
KGFKLGGPDG SGLFRAVMIH GPPGIGKTTA AHLVAKIEGY DVVERNASDA RSKKLVQDGL
QGVLETTSLL GYFAGDGKKV EESKKKLVLI MDEVDGMSAG DRGGVGALAA VCKKSEIPMI
LICNDRRLPK MKPFDYVTYD LGFRRPTTDQ IRSRIMTIIF REGLKMPKNV IDALIEGTSA
DIRQVVNMVS TAKLDETAMD YDKSKEMSKA WEKHIILKPW DIVGKILQGH MFSPTSKHTL
NDKTELYFND HELSYLMLQE NYLGTNPMRV GNHQGKERNL KLLELVDNAA ESISDGDLVD
SMIHGSQQQW SLMPTHAMFS FVRPASFVAG TMAGFKTNFP QWLGRNSSQG KLTRMIKEIQ
GHMRLRTSGD RHEIRQQYVP ILWNELVKKL EVEGKEAVPE VIDLMDSYFL TKEDFDAIME
LGVGPMDQEK IKIETQAKAT FTRLYNQQSH PIPFMKASSI VAPKQAVKEK PDLEEAIEES
DEGEVMDEPD AKKDEDEEGD ITKDKYIKQP KKKAAPKKKA TKKSAAADDD DEEEEKPKKS
KGKGRAKK
//